BEPA_SHIFL
ID BEPA_SHIFL Reviewed; 487 AA.
AC P66949; P76568;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=SF2538, S2687;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(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; AE005674; AAN44039.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP17849.1; -; Genomic_DNA.
DR RefSeq; NP_708332.1; NC_004337.2.
DR RefSeq; WP_000489667.1; NZ_UIPM01000020.1.
DR AlphaFoldDB; P66949; -.
DR SMR; P66949; -.
DR STRING; 198214.SF2538; -.
DR EnsemblBacteria; AAN44039; AAN44039; SF2538.
DR EnsemblBacteria; AAP17849; AAP17849; S2687.
DR GeneID; 1027179; -.
DR GeneID; 66673641; -.
DR KEGG; sfl:SF2538; -.
DR KEGG; sfx:S2687; -.
DR PATRIC; fig|198214.7.peg.3034; -.
DR HOGENOM; CLU_030556_0_1_6; -.
DR OMA; HLSQRHF; -.
DR OrthoDB; 1445800at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000035700"
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; 53908 MW; 92A6E6BAA370A625 CRC64;
MFRQLKKNLV ATLIAAMTIG QVAPAFADSA DTLPDMGTSA GSTLSIGQEM QMGDYYVRQL
RGSAPLINDP LLTQYINSLG MRLVSHANSV KTPFHFFLIN NDEINAFAFF GGNVVLHSAL
FRYSDNESQL ASVMAHEISH VTQRHLARAM EDQQRSAPLT 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
