ID BEPA_YERPE Reviewed; 486 AA.
AC Q8ZCC3; Q0WCJ9;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 134.
DE RecName: Full=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 Name=bepA {ECO:0000255|HAMAP-Rule:MF_00997};
GN OrderedLocusNames=YPO3069, y1412, YP_2691;
OS Yersinia pestis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CO-92 / Biovar Orientalis;
RX PubMed=11586360; DOI=10.1038/35097083;
RA Parkhill J., Wren B.W., Thomson N.R., Titball R.W., Holden M.T.G.,
RA Prentice M.B., Sebaihia M., James K.D., Churcher C.M., Mungall K.L.,
RA Baker S., Basham D., Bentley S.D., Brooks K., Cerdeno-Tarraga A.-M.,
RA Chillingworth T., Cronin A., Davies R.M., Davis P., Dougan G., Feltwell T.,
RA Hamlin N., Holroyd S., Jagels K., Karlyshev A.V., Leather S., Moule S.,
RA Oyston P.C.F., Quail M.A., Rutherford K.M., Simmonds M., Skelton J.,
RA Stevens K., Whitehead S., Barrell B.G.;
RT "Genome sequence of Yersinia pestis, the causative agent of plague.";
RL Nature 413:523-527(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KIM10+ / Biovar Mediaevalis;
RX PubMed=12142430; DOI=10.1128/jb.184.16.4601-4611.2002;
RA Deng W., Burland V., Plunkett G. III, Boutin A., Mayhew G.F., Liss P.,
RA Perna N.T., Rose D.J., Mau B., Zhou S., Schwartz D.C., Fetherston J.D.,
RA Lindler L.E., Brubaker R.R., Plano G.V., Straley S.C., McDonough K.A.,
RA Nilles M.L., Matson J.S., Blattner F.R., Perry R.D.;
RT "Genome sequence of Yersinia pestis KIM.";
RL J. Bacteriol. 184:4601-4611(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91001 / Biovar Mediaevalis;
RX PubMed=15368893; DOI=10.1093/dnares/11.3.179;
RA Song Y., Tong Z., Wang J., Wang L., Guo Z., Han Y., Zhang J., Pei D.,
RA Zhou D., Qin H., Pang X., Han Y., Zhai J., Li M., Cui B., Qi Z., Jin L.,
RA Dai R., Chen F., Li S., Ye C., Du Z., Lin W., Wang J., Yu J., Yang H.,
RA Wang J., Huang P., Yang R.;
RT "Complete genome sequence of Yersinia pestis strain 91001, an isolate
RT avirulent to humans.";
RL DNA Res. 11:179-197(2004).
CC -!- FUNCTION: Functions both as 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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM84984.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAS62881.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AL590842; CAL21671.1; -; Genomic_DNA.
DR EMBL; AE009952; AAM84984.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE017042; AAS62881.1; ALT_INIT; Genomic_DNA.
DR PIR; AD0373; AD0373.
DR RefSeq; YP_002347989.1; NC_003143.1.
DR AlphaFoldDB; Q8ZCC3; -.
DR SMR; Q8ZCC3; -.
DR IntAct; Q8ZCC3; 1.
DR STRING; 214092.YPO3069; -.
DR MEROPS; M48.023; -.
DR PaxDb; 214092-YPO3069; -.
DR DNASU; 1146359; -.
DR EnsemblBacteria; AAS62881; AAS62881; YP_2691.
DR KEGG; ype:YPO3069; -.
DR KEGG; ypk:y1412; -.
DR KEGG; ypm:YP_2691; -.
DR PATRIC; fig|1028802.3.peg.1582; -.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_030556_0_1_6; -.
DR OMA; HLSQRHF; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000000815; Chromosome.
DR Proteomes; UP000001019; Chromosome.
DR Proteomes; UP000002490; Chromosome.
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 CDD; cd07333; M48C_bepA_like; 1.
DR Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 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 PANTHER; PTHR22726:SF25; BETA-BARREL ASSEMBLY-ENHANCING PROTEASE; 1.
DR PANTHER; PTHR22726; METALLOENDOPEPTIDASE OMA1; 1.
DR Pfam; PF01435; Peptidase_M48; 1.
DR Pfam; PF14559; TPR_19; 1.
DR SUPFAM; SSF48452; TPR-like; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Periplasm; Protease;
KW Reference proteome; Signal; Zinc.
FT SIGNAL 1..19
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT CHAIN 20..486
FT /note="Beta-barrel assembly-enhancing protease"
FT /id="PRO_0000035702"
FT ACT_SITE 135
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT ACT_SITE 203
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT BINDING 134
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT BINDING 138
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT BINDING 199
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
SQ SEQUENCE 486 AA; 53418 MW; C5355EA3E14D451D CRC64;
MIATLLSSLL LTGPISAGAE TQGLLPAQDL LPDIGTSAGA TLSIDQEMAM GDFYVRQMRA
SAPLIYDPLL TQYINTLGNR LVANANSVRT PFHFYLVNND QINAFAFFGG NVVLHSALFR
YTDNESELAS VLAHEISHVT QRHLARAMEE QQRLAPLTWV GVLGSILLTM ASPQAGMAGL
SGTLAGAQQG IISFTQGNEQ EADRIGIQVL QRSGFDPQAM PNFLQKLADQ SRYVSKPPEM
LLTHPLPDSR LSDARNRANQ MKPHPTASSQ DYLFAKMRIL GMYGADENSL TPELLDKLSK
GTVREQLAAK YGQAVQLYQA KKYDEARNLL QPLLAQQPGN IWFLDLMTDI DLGQNKSAAA
IARLQNAMVK QNDEPVLQLN LANAYVQGRQ PAAAIKLLHR YTFAYPNDPN GWDLLAQATA
TQGLRDQELA ARAESLALSG KLTQAIGLLS DASARVKLGS LEQARYDARI DQLRRLNERF
RKYQKS
//
