BEPA_SALTI
ID BEPA_SALTI Reviewed; 487 AA.
AC P66951; Q8XG75;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=STY2735, t0363;
OS Salmonella typhi.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=90370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CT18;
RX PubMed=11677608; DOI=10.1038/35101607;
RA Parkhill J., Dougan G., James K.D., Thomson N.R., Pickard D., Wain J.,
RA Churcher C.M., Mungall K.L., Bentley S.D., Holden M.T.G., Sebaihia M.,
RA Baker S., Basham D., Brooks K., Chillingworth T., Connerton P., Cronin A.,
RA Davis P., Davies R.M., Dowd L., White N., Farrar J., Feltwell T.,
RA Hamlin N., Haque A., Hien T.T., Holroyd S., Jagels K., Krogh A.,
RA Larsen T.S., Leather S., Moule S., O'Gaora P., Parry C., Quail M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Stevens K., Whitehead S.,
RA Barrell B.G.;
RT "Complete genome sequence of a multiple drug resistant Salmonella enterica
RT serovar Typhi CT18.";
RL Nature 413:848-852(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700931 / Ty2;
RX PubMed=12644504; DOI=10.1128/jb.185.7.2330-2337.2003;
RA Deng W., Liou S.-R., Plunkett G. III, Mayhew G.F., Rose D.J., Burland V.,
RA Kodoyianni V., Schwartz D.C., Blattner F.R.;
RT "Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and
RT CT18.";
RL J. Bacteriol. 185:2330-2337(2003).
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; AL513382; CAD02696.1; -; Genomic_DNA.
DR EMBL; AE014613; AAO68082.1; -; Genomic_DNA.
DR RefSeq; NP_457029.1; NC_003198.1.
DR RefSeq; WP_000489630.1; NZ_WSUR01000007.1.
DR AlphaFoldDB; P66951; -.
DR SMR; P66951; -.
DR STRING; 220341.16503712; -.
DR MEROPS; M48.023; -.
DR EnsemblBacteria; AAO68082; AAO68082; t0363.
DR KEGG; stt:t0363; -.
DR KEGG; sty:STY2735; -.
DR PATRIC; fig|220341.7.peg.2773; -.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_030556_0_1_6; -.
DR OMA; HLSQRHF; -.
DR Proteomes; UP000000541; Chromosome.
DR Proteomes; UP000002670; 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; Repeat;
KW 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_0000035699"
FT REPEAT 309..342
FT /note="TPR 1"
FT REPEAT 427..460
FT /note="TPR 2"
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; 53741 MW; 593FCFCC8DBC0CCE CRC64;
MFRQLKKNLV ATLIAALALG QVAPAFADPA DTLPDMGTSA GSTLSIGQEM QMGDFYVRQL
RGSAPLINDP LLVQYINALG MRLVSHADSV KTPFHFFLIN NDEINAFAFF GGNVVLHSAL
FRYADNESQL ASVMAHEISH VTQRHLARAM EDQKRSAPLT WVGALGSILL AMASPQAGMA
ALTGTLAGTR QGMISFTQQN EQEADRIGIQ VLQRAGFDPQ AMPSFLEKLL DQARYSTRPP
EILLTHPLPE SRLADARNRA NQMRPVVVQS SADFYFAKAR ALGMYNSGRN QLTSDLLDQW
SKGNVRQQHA AQYGRALQAM EASKYDEARK TLQPLLSAEP NNAWYLDLAT DIDLGQKRAN
DAINRLKNAR DLRVNPVLQL NLANAYLQGG QPKAAETILN RYTFSHKDDG NGWDLLAQAE
AALNNRDQEL AARAESYALA GRLDQAISLL SSASAQAKLG SQQQARYDAR IDQLRQLQER
FKPYTKM
