ID   PEPB_STRA3              Reviewed;         601 AA.
AC   Q53778;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2003, sequence version 2.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=Group B oligopeptidase PepB;
DE            EC=3.4.24.-;
GN   Name=pepB; OrderedLocusNames=gbs0824;
OS   Streptococcus agalactiae serotype III (strain NEM316).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=211110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=3502 / Serotype III;
RX   PubMed=8757883; DOI=10.1128/iai.64.8.3401-3406.1996;
RA   Lin B., Averett W.F., Novak J., Chatham W.W., Hollingshead S.K.,
RA   Coligan J.E., Egan M.L., Pritchard D.G.;
RT   "Characterization of PepB, a group B streptococcal oligopeptidase.";
RL   Infect. Immun. 64:3401-3406(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEM316;
RX   PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA   Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA   Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT   "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT   neonatal disease.";
RL   Mol. Microbiol. 45:1499-1513(2002).
CC   -!- FUNCTION: Has oligopeptidase activity and degrades a variety of small
CC       bioactive peptides, including bradykinin, neurotensin, and peptide
CC       fragments of substance P and adrenocorticotropin. Also hydrolyzes the
CC       synthetic collagen-like substrate N-(3-[2-furyl]acryloyl)-Leu-Gly-Pro-
CC       Ala (FALGPA).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase M3B family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U49821; AAC44215.1; -; Genomic_DNA.
DR   EMBL; AL766847; CAD46468.1; -; Genomic_DNA.
DR   PIR; T51748; T51748.
DR   RefSeq; WP_001282905.1; NC_004368.1.
DR   AlphaFoldDB; Q53778; -.
DR   SMR; Q53778; -.
DR   STRING; 211110.gbs0824; -.
DR   MEROPS; M03.007; -.
DR   PRIDE; Q53778; -.
DR   EnsemblBacteria; CAD46468; CAD46468; CAD46468.
DR   KEGG; san:pepB; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_021290_2_0_9; -.
DR   OMA; YRQTMFA; -.
DR   Proteomes; UP000000823; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.1370.20; -; 1.
DR   InterPro; IPR013647; OligopepF_N_dom.
DR   InterPro; IPR042088; OligoPept_F_C.
DR   InterPro; IPR045090; Pept_M3A_M3B.
DR   InterPro; IPR001567; Pept_M3A_M3B_dom.
DR   InterPro; IPR004438; Peptidase_M3B.
DR   PANTHER; PTHR11804; PTHR11804; 1.
DR   Pfam; PF01432; Peptidase_M3; 1.
DR   Pfam; PF08439; Peptidase_M3_N; 1.
DR   TIGRFAMs; TIGR00181; pepF; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Metal-binding; Metalloprotease; Protease; Zinc.
FT   CHAIN           1..601
FT                   /note="Group B oligopeptidase PepB"
FT                   /id="PRO_0000078170"
FT   ACT_SITE        387
FT                   /evidence="ECO:0000250"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         393
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        39
FT                   /note="N -> D (in Ref. 1; AAC44215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        63
FT                   /note="D -> E (in Ref. 1; AAC44215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        210
FT                   /note="V -> G (in Ref. 1; AAC44215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        307
FT                   /note="S -> P (in Ref. 1; AAC44215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        324
FT                   /note="E -> K (in Ref. 1; AAC44215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        332
FT                   /note="V -> A (in Ref. 1; AAC44215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        515
FT                   /note="Y -> H (in Ref. 1; AAC44215)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        595
FT                   /note="A -> T (in Ref. 1; AAC44215)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   601 AA;  69633 MW;  5FBE051146826FA9 CRC64;
     MSDNRSHIEE KYQWDLTTVF ATDELWETEV VELTQAIDNA KGFSGHLLDS SQSLLEITEV
     ELDLSRRLEK VYVYASMKND QDTTVAKYQE FQAKATALYA KFSETFSFYE PELLQLSESD
     YQSFLLEMPD LQKYDHFFEK IFANKPHVLS QNEEELLAGA SEIFGAAGET FEILDNADMV
     FPVVKNAKGE EVELTHGNFI SLMESSDRTV RKEAYQAMYS TYEQFQHTYA KTLQTNVKSQ
     NFKARVHHYQ SARQSALSAN FIPEEVYETL IKTVNHHLPL LHRYMKLRQK VLGLDDLKMY
     DVYTPLSQMD MSFTYDEALK KSEEVLAIFG EVYSERVHRA FTERWIDVHV NKGKRSGAYS
     GGSYDTNAFM LLNWQDTLDN LYTLVHETGH SLHSTFTREN QPYVYGDYSI FLAEIASTTN
     ENILTETLLK EVKDDKNRFA ILNHYLDGFK GTIFRQTQFA EFEHAIHVAD QEGQVLTSEY
     LNNLYAELNE KYYGLTKEDN HFIQYEWARI PHFYYNYYVF QYATGFAAAN YLAERIVNGN
     PEDKEAYLNY LKAGNSDYPL NVIAKAGVDM TSADYLDAAF RVFEERLVEL ENLVAKGVHN
     D