ID C9P388_VIBME Unreviewed; 506 AA.
AC C9P388;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Putative beta-barrel assembly-enhancing protease {ECO:0000256|HAMAP-Rule:MF_00997};
DE EC=3.4.-.- {ECO:0000256|HAMAP-Rule:MF_00997};
GN ORFNames=VIB_000747 {ECO:0000313|EMBL:EEX36642.1};
OS Vibrio metschnikovii CIP 69.14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX36642.1, ECO:0000313|Proteomes:UP000005604};
RN [1] {ECO:0000313|EMBL:EEX36642.1, ECO:0000313|Proteomes:UP000005604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX36642.1,
RC ECO:0000313|Proteomes:UP000005604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA Vonstein V.;
RL Submitted (OCT-2009) 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; ACZO01000006; EEX36642.1; -; Genomic_DNA.
DR AlphaFoldDB; C9P388; -.
DR STRING; 675813.VIB_000747; -.
DR eggNOG; COG4783; Bacteria.
DR Proteomes; UP000005604; 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; 2.
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 InterPro; IPR019734; TPR_repeat.
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.
DR PROSITE; PS50005; TPR; 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 Reference proteome {ECO:0000313|Proteomes:UP000005604};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|HAMAP-Rule:MF_00997};
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00997}.
FT DOMAIN 92..276
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT REPEAT 329..362
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT ACT_SITE 156
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT ACT_SITE 224
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 155
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 159
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 220
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
SQ SEQUENCE 506 AA; 56210 MW; C16D0D1C987265ED CRC64;
MASRSVLEKD KLGALPITMK IKRSLVYLCL AATLSPLSGA YANRFGSDSI ELPDIGTVAG
STLTIDQELI YGDAYMRMLR NSRPIINDPV INEYIDALGY RLVANSDDVK TPFTFFMIRD
RNINAFAFFG GYIALHSGLL LHAQSESELA SVMAHEIAHV TQRHLARSME EQARRSPATI
AALAGSLLLA IAAPQAGIAA ITATTAGSMQ SQINYTRSNE KEADRFGIAT LAKAGFDVHA
MPRFFGRLAD EYRYASTPPP MLLTHPLPED RITDSRSRAQ QFPSVSVAPS LNYHLTRSRV
VARYAGINSE AALDWFKRNQ RKADPGMAAA FDYGKALVYL DTKQYDEAES RLKKLLQSHP
DNNFYLDAMS DLLVDTERAT EAQSMLAQAL QRKPNNPVLV INYANVLIKD EKFSEAIRIL
QRYTHERPND VNGWHLLAEA NSRSGNSAED LAARAEIFAL GANWNKAIQF YTQASQLAPL
GSLQQARYDA RLDQLMVQRD RFLALR
//
