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Porphyromonas gingivalis Search Results

Record: 1 of 1  
MiniMap IGR0390 IGR0392 IGR0384 IGR0391 IGR0385 IGR0389 IGR0386 IGR0388 IGR0387 PG0464 gmk, - PG0466 PG0463 PG0465 PG0461.1 smpB, - PG0458 lipA, - PG0460 dppIV, - PG0459 rgpB,prtRII,rgp-2,prpR2, - PG0461 PG0464 gmk, - PG0466 PG0463 PG0465 PG0461.1 smpB, - PG0458 lipA, - PG0460 dppIV, - PG0459 rgpB,prtRII,rgp-2,prpR2, - PG0461 PG0464 gmk, - PG0466 PG0463 PG0465 PG0462 PG0462 PG0461.1 smpB, - PG0458 lipA, - PG0460 dppIV, - PG0459 rgpB,prtRII,rgp-2,prpR2, - PG0461


LANL Gene ID: PG0461

GenBank Locus Tag: PG0506

DNA Molecule Name:
1  

GenBank ID:
34540322

Gene Name:
rgpB  prtRII  rgp-2  prpR2  

Definition:
arginine-specific cysteine proteinase: gingipain R2

Cellular Location:
Periplasm, Cytoplasm, Extracellular [Evidence]

Gene Start:
545476

Gene Stop:
547683

Gene Length:
2208

Molecular Weight*:
80961

pI*:
5.50

Net Charge*:
-9.33

EC:
3.4.22.37  

Functional Class:
Protein fate; Degradation of proteins, peptides and glycopeptides  

Gene Ontology:
Biological process
  GO:0006508    proteolysis

Molecular function
  GO:0004197    cysteine-type endopeptidase activity
  GO:0008233    peptidase activity
  GO:0008234    cysteine-type peptidase activity


Pathway: pathway table

Primary Evidence:
See href="http://linker.lanl.gov/readonly/oragen/bacteria/pgin/hemagglutinin/summ_hemag.htm">Proteases/Hemagglutinin Analysis


Veith,P., Talbo,G., Slakeski,N., Dashper,S., Moore,C.,Paolini,R., Reynolds,E., Major outer membrane proteins and proteolytic processing of RgpA, and Kgp of Porphyromonas gingivalis W50, Biochem J. 2002 (in press).

Slakeski,N., Bhogal,P.S., O'Brien-Simpson,N.M. and Reynolds,E.C.
Characterization of a second cell-associated Arg-specific cysteine proteinase of Porphyromonas gingivalis and identification of an adhesin-binding motif involved in association of the prtR and prtK proteinases and adhesins into large complexes. Microbiology 144 (Pt 6), 1583-1592 (1998). PubMed: 9639929.

Gharbia,S.E. and Shah,H.N.
Molecular analysis of surface-associated enzymes of Porphyromonas
gingivalis
Clin. Infect. Dis. In press

Aduse-Opoku,J., Muir,J., Slaney,J.M., Rangarajan,M. and Curtis,M.A.
Characterization, genetic analysis, and expression of a protease
antigen (PrpRI) of Porphyromonas gingivalis W50
Infect. Immun. 63 (12), 4744-4754 (1995)

Rangarajan,M., Aduse-Opoku,J., Slaney,J.M., Young,K.A. and
Curtis,M.A.
The prpR1 and the prR2 arginine-specific protease genes of
Porphyromonas gingivalis W50 produce five biochemically distinct
enzymes
Mol. Microbiol. 23 (1997) In press

Kirszbaum,L., Sotiropoulos,C., Jackson,C., Cleal,S., Slakeski,N.
and Reynolds,E.C.
Complete nucleotide sequence of a gene prtR of Porphyromonas
gingivalis W50 encoding a 132 kDa protein that contains an
arginine-specific thiol endopeptidase domain and a haemagglutinin
domain.
Biochem. Biophys. Res. Commun. 207 (1), 424-431 (1995)

Pike,R., McGraw,W., Potempa,J. and Travis,J.
Lysine- and arginine-specific proteinases from Porphyromonas
gingivalis. Isolation, characterization, and evidence for the
existence of complexes with hemagglutinins
J. Biol. Chem. 269 (1), 406-411 (1994)

Pavloff,N., Potempa,J., Pike,R.N., Prochazka,V., Kiefer,M.C.,
Travis,J. and Barr,P.J.
Molecular cloning and structural characterization of the
Arg-gingipain proteinase of Porphyromonas gingivalis. Biosynthesis as a proteinase-adhesin polyprotein.
J. Biol. Chem. 270 (3), 1007-1010 (1995)

Aduse-Opoku,J., Slaney,J.M., Rangarajan,M., Muir,J., Young,K.A. and Curtis,M.A.
The Tla protein of Porphyromonas gingivalis W50: a homolog of the
RI protease precursor (PrpRI) is an outer membrane receptor
required for growth on low levels of hemin
J. Bacteriol. 179 (15), 4778-4788 (1997)

Nakayama,K.
Domain-specific rearrangement between the two
Arg-gingipain-encoding genes in Porphyromonas gingivalis: possible involvement of nonreciprocal recombination.
Microbiol. Immunol. 41 (3), 185-196 (1997)

Nakayama,K., Kadowaki,T., Okamoto,K. and Yamamoto,K.
Construction and characterization of arginine-specific cysteine
proteinase (Arg-gingipain)-deficient mutants of Porphyromonas
gingivalis. Evidence for significant contribution of Arg-gingipain to virulence.
J. Biol. Chem. 270 (40), 23619-23626 (1995)

Comment:
Gingipain R2 is a thiol protease thought to be responsible for intracellular protein degradation associated with peridontal disease. This protein, unlike the R1 form (PG1768) does not include a C-terminal adhesin region with hagA hemagglutinin repeats.
Gene nomenclature and strains (from Lamont and Jenkinson): rgp-2 (HG66), rgpB (ATCC 33277), prtII (W50), prpR2 (W50).


Veith et al. (2002) identified this protein by two-dimensional gel electrophoresis and peptide mass fingerprinting of outer membranes prepared from strain W50. They present the following results: This protein together with PG1838, PG1570 and the C-terminal domain of PG1768 migrate as vertical streaks on 2D-PAGE at a MW 13-42 kDa higher than that calculated from their gene sequences. The electrophoretic behaviour of these proteins together with their immunoreactivity with a monoclonal antibody that recognises LPS is consistent with a modification that could anchor the proteins to the outer membrane. The proposed LPS-attachment site is in the conserved C-terminal 50 amino acid residues of each of these proteins. Based on signal peptide sequence comparisons to PG0626, PG0627, PG1592, PG1840, PG0836, PG0023, PG1893, the mature N-terminus of this protein is predicted to be pyroglutamate.

TIGR ID: PG0506

Proteomic Data: Proteomic Data Search
TIGR Annotationarginine-specific cysteine proteinase, GroupM (protein fate)
ORF #PG-PP/PG-PPC1PG-PP/PG-PPC2
Spectral CountPeptide IntensitySpectral CountPeptide Intensity
ProqValProqValProqValProqVal
TIGRPG0506-0.437.8e-14-0.340.055-0.800-0.340.055
LANLPG04610.740.790.570.56
ConsensusSP1IP1SP2IP2

Human Oral Microbiome Database:
View in HOMD Genome Viewer

 Blast Summary:  PSI-Blast Search
This sequence corresponds to the previously sequenced AF007124 from P.gingivalis strain W50, a predicted prtRII gene. See also U85038 and D64081. No significant hits in gapped BLAST except to paralogs.

See also POYRGPB.

 Top Blast Hits:  Updated monthly
Click here to view the entire PsiBlast results.
 gi|34540322|ref|NP_904801.1|  arginine-specific cysteine pro...  1453   0.0  
 gi|1814394|gb|AAB41892.1|  arginine-specific cysteine protei...  1428   0.0  
 gi|1246379|dbj|BAA10963.1|  arginine-specific cysteine prote...  1425   0.0  
 gi|34541613|ref|NP_906092.1|  hemagglutinin protein HagE [Po...  1133   0.0  
 gi|1813996|emb|CAA57997.1|  protease precursor [Porphyromona...  1132   0.0  
 gi|557068|gb|AAA69539.1|  Arg-gingipain-1 proteinase             1131   0.0  
 gi|1066835|gb|AAC18876.1|  arginine-specific thiol protease ...  1131   0.0  
 gi|2827775|sp|P28784|CPG1_PORGI  Gingipain R1 precursor (Gin...  1130   0.0  
 gi|4103639|gb|AAD01810.1|  hemagglutinin/protease [Porphyrom...  1112   0.0  
 gi|7245522|pdb|1CVR|A  Chain A, Crystal Structure Of The Arg...   862   0.0


InterPro Summary:  InterProScan

InterPro
IPR001769
Family
Peptidase C25, gingipain
PF01364 [230-578]T 0.0 PF01364 Peptidase_C25 Peptidase_C25
InterPro
IPR005536
Domain
Peptidase C25, C-terminal ig-like region
PF03785 [580-660]T 8.000026593468089E-54 PF03785 Peptidase_C25_C Peptidase_C25_C
InterPro
IPR012600
Domain
Propetide, peptidase C25
PF08126 [25-229]T 0.0 PF08126 Propeptide_C25 Propeptide_C25
InterPro
IPR013783
Domain
Immunoglobulin-like fold
G3DSA:2.60.40.10 [579-664]T 1.30000495407324E-42 G3DSA:2.60.40.10 Ig-like_fold Ig-like_fold
InterPro
IPR014756
Domain
Immunoglobulin E-set
SSF81296 [580-661]T 3.6E-43 SSF81296 Ig_E-set Ig_E-set
noIPR
unintegrated
unintegrated
G3DSA:3.40.50.10390 [230-346]T 1.3999927719513797E-71 G3DSA:3.40.50.10390 G3DSA:3.40.50.10390 G3DSA:3.40.50.10390
G3DSA:3.40.50.1460 [347-577]T 3.999985441393791E-91 G3DSA:3.40.50.1460 G3DSA:3.40.50.1460 G3DSA:3.40.50.1460
SSF52129 [230-579]T 1.7E-117 SSF52129 SSF52129 SSF52129


COGS Summary:  COGS Search
No hit to the COGs database.
Blocks Summary:  Blocks Search
***** PF01364 (Peptidase family C25) with a combined E-value of 7.1e-263.
    PF01364A    46-95
    PF01364B    245-252
    PF01364C    260-313
    PF01364D    373-410
    PF01364E    491-541
    PF01364F    610-663
    PF01364G    694-732


 ProDom Summary:  Protein Domain Search
Residues 649-736 are identical to a (PROTEASE PRECURSOR THIOL SIGNAL) protein domain (PD004371 which is seen in CPG2_PORGI.

Residues 3-219 are identical to a (PROTEASE CYSTEINE PRECURSOR THIOL) protein domain (PD005390 which is seen in O33441_PORGI.

Residues 439-648 are identical to a (PROTEASE PROTEINASE CYSTEINE PRECURSOR) protein domain (PD007636 which is seen in O33441_PORGI.

Residues 221-438 are identical to a (PROTEASE THIOL CYSTEINE PRECURSOR) protein domain (PD005006 which is seen in O33441_PORGI.


Paralogs:  Local Blast Search
PG0461 is paralogous to PG1768, arginine-specific cysteine proteinase (gingipain R1). Residues 3-662 are 84% similar to residues 2-659 of PG1768. Weaker similarity (24%) is seen to PG1605, although PG0461 does not contain the hemagglutinin repeats. Short domains of PH0461 show similarity to PG1606, PG1602, PG1922, PG0022, PG1164, PG0375 and PG1570.

Pfam Summary:  Pfam Search
Residues 230 to 578 (E-value = 3.3e-275) place PG0461 in the Peptidase_C25 family which is described as Peptidase family C25 (PF01364)
Residues 580 to 660 (E-value = 1.1e-56) place PG0461 in the Peptidase_C25_C family which is described as Peptidase family C25, C terminal ig-like domain (PF03785)

 Structural Feature(s):
Feature Type  Start  Stop
cleavable signal  
1  
24
gram negative signal  
1  
24
non-globular  
605  
693

Top PDB Hits:
No significant hits to the PDB database (E-value < E-10).

Gene Protein Sequence:
MKKNFSRIVSIVAFSSLLGGMAFAQPAERGRNPQVRLLSAEQSMSKVQFR
MDNLQFTGVQTSKGVAQVPTFTEGVNISEKGTPILPILSRSLAVSETRAM
KVEVVSSKFIEKKDVLIAPSKGVISRAENPDQIPYVYGQSYNEDKFFPGE
IATLSDPFILRDVRGQVVNFAPLQYNPVTKTLRIYTEIVVAVSETAEAGQ
NTISLVKNSTFTGFEDIYKSVFMNYEATRYTPVEEKENGRMIVIVPKKYE
EDIEDFVDWKNQRGLRTEVKVAEDIASPVTANAIQQFVKQEYEKEGNDLT
YVLLVGDHKDIPAKITPGIKSDQVYGQIVGNDHYNEVFIGRFSCESKEDL
KTQIDRTIHYERNITTEDKWLGQALCIASAEGGPSADNGESDIQHENIIA
NLLTQYGYTKIIKCYDPGVTPKNIIDAFNGGISLANYTGHGSETAWGTSH
FGTTHVKQLTNSNQLPFIFDVACVNGDFLYNVPCFAEALMRAQKDGKPTG
TVAIIASTINQSWASPMRGQDEMNEILCEKHPNNIKRTFGGVTMNGMFAM
VEKYKKDGEKMLDTWTVFGDPSLLVRTLVPTKMQVTAPANISASAQTFEV
ACDYNGAIATLSDDGDMVGTAIVKDGKAIIKLNESIADETNLTLTVVGYN
KVTVIKDVKVEGTSIADVANDKPYTVAVSGKTITVESPAAGLTIFDMNGR
RVATAKNRMVFEAQNGVYAVRIATEGKTYTEKVIVK

Gene Nucleotide Sequence:  Sequence Viewer
ATGAAAAAGAATTTTAGCAGGATCGTTTCGATCGTAGCATTCTCCTCTCT
GTTGGGAGGAATGGCGTTTGCACAGCCGGCAGAGCGCGGTCGCAACCCAC
AAGTACGACTGCTCTCCGCTGAGCAGTCTATGTCCAAGGTGCAATTCCGT
ATGGACAATCTTCAGTTCACAGGCGTACAGACCTCCAAAGGGGTAGCTCA
GGTGCCTACCTTCACCGAAGGTGTCAATATCTCGGAGAAAGGTACGCCTA
TATTGCCCATTCTTTCCCGTTCTCTTGCCGTTTCTGAAACACGTGCGATG
AAGGTAGAGGTAGTTTCTTCCAAATTCATCGAAAAGAAGGATGTGCTGAT
CGCTCCCTCTAAAGGTGTTATCTCTCGCGCTGAAAATCCTGATCAAATCC
CCTACGTGTACGGACAGAGCTATAATGAAGACAAGTTCTTCCCGGGCGAA
ATCGCTACGCTGAGCGATCCTTTCATCCTGCGCGATGTACGTGGTCAGGT
AGTAAACTTTGCTCCGCTCCAGTATAACCCTGTTACAAAGACCCTCCGCA
TCTATACGGAAATCGTTGTAGCTGTGAGCGAAACAGCTGAAGCGGGCCAG
AATACGATTAGCTTGGTTAAGAACAGTACTTTCACAGGCTTCGAAGATAT
CTATAAGAGCGTCTTCATGAATTATGAAGCTACGCGCTATACGCCTGTTG
AAGAAAAGGAGAATGGTCGTATGATCGTCATCGTACCCAAAAAATATGAG
GAAGATATTGAAGATTTCGTTGATTGGAAAAACCAACGCGGTCTCCGTAC
CGAGGTGAAAGTGGCAGAAGATATTGCTTCTCCCGTTACAGCTAATGCTA
TTCAGCAGTTCGTTAAGCAAGAATACGAGAAAGAAGGTAATGATTTGACC
TATGTTCTTTTGGTTGGCGATCACAAAGATATTCCTGCCAAAATTACTCC
GGGGATCAAATCCGACCAGGTATATGGACAAATAGTAGGTAATGACCACT
ACAACGAAGTCTTCATCGGTCGTTTCTCATGTGAGAGCAAAGAGGATCTG
AAGACACAAATCGATCGGACTATTCACTATGAGCGCAATATAACCACGGA
AGACAAATGGCTCGGTCAGGCTCTTTGTATTGCTTCGGCTGAAGGAGGCC
CATCCGCAGACAATGGTGAAAGTGATATCCAGCATGAGAATATAATCGCC
AATCTGCTTACCCAGTATGGCTATACCAAGATTATCAAATGTTATGATCC
GGGAGTAACTCCTAAAAACATTATTGATGCTTTCAACGGAGGAATCTCGT
TGGCCAACTATACGGGCCACGGAAGCGAAACAGCTTGGGGTACGTCTCAC
TTCGGCACCACTCATGTGAAGCAGCTTACCAACAGCAACCAGCTACCGTT
TATTTTCGACGTAGCTTGTGTGAATGGCGATTTCCTGTACAACGTACCAT
GTTTCGCAGAAGCCCTGATGCGTGCACAAAAAGATGGTAAACCGACAGGT
ACTGTTGCTATCATAGCGTCTACGATCAACCAGTCTTGGGCTTCTCCTAT
GCGCGGGCAGGATGAGATGAACGAAATTCTGTGCGAAAAACACCCGAACA
ACATCAAGCGTACTTTCGGAGGTGTCACCATGAACGGTATGTTTGCTATG
GTGGAAAAGTATAAAAAGGATGGTGAGAAGATGCTCGACACATGGACTGT
ATTCGGCGACCCCTCGCTGCTCGTTCGTACACTTGTCCCGACCAAAATGC
AGGTTACGGCTCCGGCAAATATCTCTGCCTCTGCACAGACATTCGAAGTA
GCTTGCGACTATAACGGTGCTATTGCTACGCTCTCTGACGATGGTGATAT
GGTCGGCACTGCTATCGTGAAAGACGGTAAGGCTATCATCAAATTAAATG
AGAGTATCGCTGATGAAACGAACTTGACGCTCACCGTAGTAGGATACAAT
AAGGTTACTGTGATAAAGGATGTGAAAGTGGAAGGTACATCTATTGCCGA
CGTAGCCAATGATAAGCCTTATACTGTAGCTGTATCAGGTAAGACGATAA
CTGTAGAAAGTCCTGCTGCCGGGCTGACGATCTTCGATATGAACGGCCGT
CGTGTAGCTACTGCTAAAAACCGCATGGTATTCGAAGCACAAAACGGCGT
GTATGCCGTTCGCATCGCTACTGAAGGCAAGACGTATACAGAAAAGGTTA
TAGTGAAG

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