ID A0A285KEC6_9ENTR Unreviewed; 487 AA.
AC A0A285KEC6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Beta-barrel assembly-enhancing protease {ECO:0000256|HAMAP-Rule:MF_00997};
DE EC=3.4.-.- {ECO:0000256|HAMAP-Rule:MF_00997};
DE Flags: Precursor;
GN Name=bepA {ECO:0000256|HAMAP-Rule:MF_00997};
GN ORFNames=SAMN02744775_02463 {ECO:0000313|EMBL:SNY70984.1};
OS Enterobacter sp. CC120223-11.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Enterobacter.
OX NCBI_TaxID=1378073 {ECO:0000313|EMBL:SNY70984.1, ECO:0000313|Proteomes:UP000219512};
RN [1] {ECO:0000313|EMBL:SNY70984.1, ECO:0000313|Proteomes:UP000219512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CC120223-11 {ECO:0000313|EMBL:SNY70984.1,
RC ECO:0000313|Proteomes:UP000219512};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-2017) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00997}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00997};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00997};
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000256|HAMAP-Rule:MF_00997}.
CC -!- SIMILARITY: Belongs to the peptidase M48 family. BepA subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00997}.
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DR EMBL; OBEF01000009; SNY70984.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A285KEC6; -.
DR OrthoDB; 9810445at2; -.
DR Proteomes; UP000219512; Unassembled WGS sequence.
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 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00997};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00997};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW Rule:MF_00997};
KW Periplasm {ECO:0000256|ARBA:ARBA00022764, ECO:0000256|HAMAP-Rule:MF_00997};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00997};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00997};
KW TPR repeat {ECO:0000256|ARBA:ARBA00022803};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00997}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT CHAIN 28..487
FT /note="Beta-barrel assembly-enhancing protease"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT /id="PRO_5013409042"
FT DOMAIN 75..259
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 137
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT ACT_SITE 205
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 136
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
SQ SEQUENCE 487 AA; 53690 MW; ECF542C683E41C75 CRC64;
MFRQLKKTLV ATLIASLTLG QALPAFADTA DSLPDMGTTA GSTLSIGQEM QMGDYYVRQL
RGSAPLINDP LLVQYINGLG MRLVSHANSV RTPFHFFLIN NDELNAFAFF GGNVVLHSAL
FRYADTESQL ASVMAHEISH VTQRHLARAM EDQKRNAPLT WVGALGSILL AMASPQAGMA
ALTGTLAGTQ QGLISFTRQN EEEADRIGIQ VLQRSGFDPQ GMPQFMDKLM DQSRYSSRPP
EMLLTHPLPE SRLSDARNRA NQMRPVVVQS SEDFYMAKAR TLGMYNNGQN QLGSDLLDNW
SKGNIREQHA AQYGRALQAM EASNYAEASK QLQPLLTANP QNAWYLDLAT DISLGQKKNA
EAVNRLKAAK DLRTNPVLQL NLANALLQSG NPGEAATLLN RYTFTYKDDT NGWDLLAQAE
GQLGNRDQEL AARAEGMALV GRLDQAISLL SSASSQVKLG SLQQARYDAR IDQFRQLQDT
FKPYMKM
//
