ID   BEPA_VIBCH              Reviewed;         484 AA.
AC   Q9KQ40;
DT   05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Putative beta-barrel assembly-enhancing protease {ECO:0000255|HAMAP-Rule:MF_00997};
DE            EC=3.4.-.- {ECO:0000255|HAMAP-Rule:MF_00997};
DE   Flags: Precursor;
GN   OrderedLocusNames=VC_2164;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- FUNCTION: Functions as both a chaperone and a metalloprotease.
CC       Maintains the integrity of the outer membrane by promoting either the
CC       assembly or the elimination of outer membrane proteins, depending on
CC       their folding state. {ECO:0000255|HAMAP-Rule:MF_00997}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00997};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00997};
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00997}.
CC   -!- SIMILARITY: Belongs to the peptidase M48 family. BepA subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00997}.
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DR   EMBL; AE003852; AAF95309.1; -; Genomic_DNA.
DR   PIR; E82110; E82110.
DR   RefSeq; NP_231795.1; NC_002505.1.
DR   RefSeq; WP_000667946.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KQ40; -.
DR   SMR; Q9KQ40; -.
DR   STRING; 243277.VC_2164; -.
DR   MEROPS; M48.023; -.
DR   DNASU; 2613300; -.
DR   EnsemblBacteria; AAF95309; AAF95309; VC_2164.
DR   GeneID; 57740779; -.
DR   KEGG; vch:VC_2164; -.
DR   PATRIC; fig|243277.26.peg.2065; -.
DR   eggNOG; COG4783; Bacteria.
DR   HOGENOM; CLU_030556_1_1_6; -.
DR   OMA; HLSQRHF; -.
DR   BioCyc; VCHO:VC2164-MON; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0061077; P:chaperone-mediated protein folding; IEA:InterPro.
DR   GO; GO:0051603; P:proteolysis involved in protein catabolic process; IBA:GO_Central.
DR   Gene3D; 1.25.40.10; -; 1.
DR   HAMAP; MF_00997; Protease_BepA; 1.
DR   InterPro; IPR001915; Peptidase_M48.
DR   InterPro; IPR030873; Protease_BepA.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   Pfam; PF01435; Peptidase_M48; 1.
DR   Pfam; PF13181; TPR_8; 1.
DR   SMART; SM00028; TPR; 3.
DR   SUPFAM; SSF48452; SSF48452; 1.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Metalloprotease; Periplasm; Protease;
KW   Reference proteome; Repeat; Signal; TPR repeat; Zinc.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT   CHAIN           24..484
FT                   /note="Putative beta-barrel assembly-enhancing protease"
FT                   /id="PRO_0000035701"
FT   REPEAT          307..340
FT                   /note="TPR 1"
FT   REPEAT          341..374
FT                   /note="TPR 2"
FT   REPEAT          376..408
FT                   /note="TPR 3"
FT   REPEAT          426..459
FT                   /note="TPR 4"
FT   ACT_SITE        134
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT   ACT_SITE        202
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT   BINDING         133
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT   BINDING         137
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT   BINDING         198
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
SQ   SEQUENCE   484 AA;  54104 MW;  92D514E468AA9B2E CRC64;
     MKFFPTRTLL CLCIAAPCLP AIAQNDPIEL PDIGTVAGST LTIDQELIYG DAYMRMLRNN
     QPVINDPVLN EYIDNLGHRL VASANDVKTP FTFFMIRDRN INAFAFFGGY VALHSGLFLH
     AQSESELASV MAHEIAHVTQ RHLARSMEEQ ARRSPATIAA LAGSLLLAIA APEAGIAAIN
     ATMAGSIQGQ INYTRSNEKE ADRFGIATLA KAGFDANAMP QFFTRLADEY RYASKPPPML
     LTHPLPEDRI TDSRERARQY PPLKLAPHLD YHLARARIIA RYAGIDADAA LDWFARSEKK
     IDATLQPSIQ YGKALVYLDL KQFDKAEPLL TQLVKEQPDN HFYLDAISDL YIELKQADKA
     QSLLEKALKQ TPNNSVLTIN YANVLLKQDK FTDAIRILQR YTHDNPNDIN GWQLLSEANS
     RLGNSAEDLA ARGEIMALQA NWNKAIQFYT QASQLVELGS LAQARYDARI DQLMVQRERF
     LSLQ