BEPA_ECOLI
ID BEPA_ECOLI Reviewed; 487 AA.
AC P66948; P76568; Q2MAI2;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 132.
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=b2494, JW2479;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP FUNCTION, INTERACTION WITH LOIP, AND SUBCELLULAR LOCATION.
RX PubMed=22491786; DOI=10.1039/c2mb05506f;
RA Lutticke C., Hauske P., Lewandrowski U., Sickmann A., Kaiser M.,
RA Ehrmann M.;
RT "E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.";
RL Mol. Biosyst. 8:1775-1782(2012).
RN [4]
RP FUNCTION AS A CHAPERONE AND A PROTEASE, ACTIVITY REGULATION, INTERACTION
RP WITH BAMA, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE, GENE NAME, AND
RP MUTAGENESIS OF HIS-136 AND GLU-137.
RC STRAIN=K12;
RX PubMed=24003122; DOI=10.1073/pnas.1312012110;
RA Narita S., Masui C., Suzuki T., Dohmae N., Akiyama Y.;
RT "Protease homolog BepA (YfgC) promotes assembly and degradation of beta-
RT barrel membrane proteins in Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:E3612-E3621(2013).
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. Promotes disulfide rearrangement of LptD during
CC its biogenesis, and proteolytic degradation of LptD and BamA when their
CC proper assembly is compromised. May facilitate membrane attachment of
CC LoiP under unfavorable conditions. {ECO:0000255|HAMAP-Rule:MF_00997,
CC ECO:0000269|PubMed:22491786, ECO:0000269|PubMed:24003122}.
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 -!- ACTIVITY REGULATION: Protease activity is inhibited by the metal
CC chelating reagents 1,10-phenanthroline and EDTA.
CC {ECO:0000269|PubMed:24003122}.
CC -!- SUBUNIT: Interacts with BamA and LoiP. {ECO:0000269|PubMed:22491786,
CC ECO:0000269|PubMed:24003122}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000255|HAMAP-Rule:MF_00997,
CC ECO:0000269|PubMed:22491786, ECO:0000269|PubMed:24003122}. Note=A
CC significant amount of BepA is membrane-associated. This localization
CC could result from interaction with the BAM complex.
CC -!- DISRUPTION PHENOTYPE: Disruption sensitizes cells to multiple drugs.
CC {ECO:0000269|PubMed:24003122}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family. BepA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_00997}.
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DR EMBL; U00096; AAC75547.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76724.1; -; Genomic_DNA.
DR PIR; E65025; E65025.
DR RefSeq; NP_416989.1; NC_000913.3.
DR RefSeq; WP_000489667.1; NZ_STEB01000011.1.
DR PDB; 5XI8; X-ray; 1.70 A; A=310-482.
DR PDB; 6AIT; X-ray; 2.60 A; A/B/C/D/E/F=45-482.
DR PDB; 6SAR; X-ray; 2.18 A; A=1-487.
DR PDBsum; 5XI8; -.
DR PDBsum; 6AIT; -.
DR PDBsum; 6SAR; -.
DR AlphaFoldDB; P66948; -.
DR SMR; P66948; -.
DR BioGRID; 4261434; 45.
DR DIP; DIP-28089N; -.
DR IntAct; P66948; 3.
DR STRING; 511145.b2494; -.
DR MEROPS; M48.023; -.
DR jPOST; P66948; -.
DR PaxDb; P66948; -.
DR PRIDE; P66948; -.
DR EnsemblBacteria; AAC75547; AAC75547; b2494.
DR EnsemblBacteria; BAE76724; BAE76724; BAE76724.
DR GeneID; 66673641; -.
DR GeneID; 947029; -.
DR KEGG; ecj:JW2479; -.
DR KEGG; eco:b2494; -.
DR PATRIC; fig|511145.12.peg.2590; -.
DR EchoBASE; EB3951; -.
DR eggNOG; COG4783; Bacteria.
DR HOGENOM; CLU_030556_0_1_6; -.
DR InParanoid; P66948; -.
DR OMA; HLSQRHF; -.
DR PhylomeDB; P66948; -.
DR BioCyc; EcoCyc:G7311-MON; -.
DR BioCyc; MetaCyc:G7311-MON; -.
DR PRO; PR:P66948; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; TAS:EcoCyc.
DR GO; GO:0046872; F:metal ion binding; ISM:EcoCyc.
DR GO; GO:0004222; F:metalloendopeptidase activity; IDA:EcoCyc.
DR GO; GO:0003756; F:protein disulfide isomerase activity; IMP:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR GO; GO:0061077; P:chaperone-mediated protein folding; IMP:EcoCyc.
DR GO; GO:0043165; P:Gram-negative-bacterium-type cell outer membrane assembly; IMP:EcoCyc.
DR GO; GO:0051603; P:proteolysis involved in protein catabolic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Metal-binding; Metalloprotease; Periplasm;
KW Protease; 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_0000035696"
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"
FT MUTAGEN 136
FT /note="H->R: Lack of protease activity. Increases
FT sensitivity to erythromycin."
FT /evidence="ECO:0000269|PubMed:24003122"
FT MUTAGEN 137
FT /note="E->Q: Lack of protease activity. Increases
FT sensitivity to erythromycin."
FT /evidence="ECO:0000269|PubMed:24003122"
FT HELIX 46..61
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 70..84
FT /evidence="ECO:0007829|PDB:6SAR"
FT STRAND 95..99
FT /evidence="ECO:0007829|PDB:6SAR"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:6SAR"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:6SAR"
FT STRAND 113..117
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 119..123
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 127..142
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 145..150
FT /evidence="ECO:0007829|PDB:6AIT"
FT TURN 151..153
FT /evidence="ECO:0007829|PDB:6AIT"
FT HELIX 161..173
FT /evidence="ECO:0007829|PDB:6AIT"
FT HELIX 198..214
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 221..235
FT /evidence="ECO:0007829|PDB:6SAR"
FT STRAND 236..238
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 242..245
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 250..262
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 272..284
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:6SAR"
FT HELIX 310..321
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 343..355
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 359..367
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 370..374
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 376..388
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 392..405
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 410..422
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 426..439
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 443..456
FT /evidence="ECO:0007829|PDB:5XI8"
FT HELIX 462..479
FT /evidence="ECO:0007829|PDB:5XI8"
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
