BEPA_ECO57
ID BEPA_ECO57 Reviewed; 487 AA.
AC Q8XAD2;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
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}; Synonyms=yfgC;
GN OrderedLocusNames=Z3757, ECs3356;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG57604.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB36779.1; -; Genomic_DNA.
DR PIR; D91048; D91048.
DR PIR; H85892; H85892.
DR RefSeq; NP_311383.1; NC_002695.1.
DR RefSeq; WP_000489651.1; NZ_SEKU01000005.1.
DR AlphaFoldDB; Q8XAD2; -.
DR SMR; Q8XAD2; -.
DR STRING; 155864.EDL933_3649; -.
DR MEROPS; M48.023; -.
DR EnsemblBacteria; AAG57604; AAG57604; Z3757.
DR EnsemblBacteria; BAB36779; BAB36779; ECs_3356.
DR GeneID; 915227; -.
DR KEGG; ece:Z3757; -.
DR KEGG; ecs:ECs_3356; -.
DR PATRIC; fig|386585.9.peg.3505; -.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_030556_0_1_6; -.
DR OMA; HLSQRHF; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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:0006508; P:proteolysis; IEA:UniProtKB-KW.
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 Pfam; PF01435; Peptidase_M48; 1.
DR SUPFAM; SSF48452; SSF48452; 1.
PE 3: Inferred from homology;
KW Hydrolase; Metal-binding; Metalloprotease; Periplasm; Protease;
KW Reference proteome; Repeat; Signal; TPR repeat; Zinc.
FT SIGNAL 1..27
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT CHAIN 28..487
FT /note="Beta-barrel assembly-enhancing protease"
FT /id="PRO_0000035697"
FT REPEAT 309..342
FT /note="TPR 1"
FT REPEAT 344..376
FT /note="TPR 2"
FT REPEAT 377..409
FT /note="TPR 3"
FT REPEAT 427..460
FT /note="TPR 4"
FT ACT_SITE 137
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00997"
SQ SEQUENCE 487 AA; 53935 MW; 2A9EE2BEABB86DD4 CRC64;
MFRQLKKNLV ATLIAAMTIG QVAPAFADSA DTLPDMGTSA GSTLSIGQEM QMGDYYVRQL
RGSAPLINDP LLTQYINSLG MRLVSHANSV KTPFHFFLIN NDEINAFAFF GGNVVLHSAL
FRYSDNESQL ASVMAHEISH VTQRHLARAM EDQQRNAPLT WVGALGSILL AMASPQAGMA
ALTGTLAGTR QGMISFTQQN EQEADRIGIQ VLQRSGFDPQ AMPTFLEKLL DQARYSSRPP
EILLTHPLPE SRLADARNRA NQMRPMVVQS SEDFYLAKAR TLGMYNSGRN QLTSDLLDEW
AKGNVRQQRA AQYGRALQAM EANKYDEARK TLQPLLAAEP GNAWYLDLAT DIDLGQNKAN
EAINRLKNAR DLRTNPVLQL NLANAYLQGG QPQEAANILN RYTFNNKDDS NGWDLLAQAE
AALNNRDQEL AARAEGYALA GRLDQAISLL SSASSQVKLG SLQQARYDAR IDQLRQLQER
FKPYTKM
