ID A6D3F5_9VIBR Unreviewed; 483 AA.
AC A6D3F5;
DT 24-JUL-2007, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
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};
DE Flags: Precursor;
GN ORFNames=VSAK1_07389 {ECO:0000313|EMBL:EDL52830.1};
OS Vibrio mediterranei AK1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=391591 {ECO:0000313|EMBL:EDL52830.1, ECO:0000313|Proteomes:UP000003769};
RN [1] {ECO:0000313|EMBL:EDL52830.1, ECO:0000313|Proteomes:UP000003769}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AK1 {ECO:0000313|EMBL:EDL52830.1,
RC ECO:0000313|Proteomes:UP000003769};
RA Rosenberg E., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUN-2007) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDL52830.1}.
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DR EMBL; ABCH01000025; EDL52830.1; -; Genomic_DNA.
DR RefSeq; WP_006072846.1; NZ_ABCH01000025.1.
DR AlphaFoldDB; A6D3F5; -.
DR MEROPS; M48.023; -.
DR GeneID; 64087081; -.
DR Proteomes; UP000003769; 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 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 Pfam; PF13174; TPR_6; 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 Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00997}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT CHAIN 26..483
FT /note="Putative beta-barrel assembly-enhancing protease"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT /id="PRO_5009006996"
FT DOMAIN 68..255
FT /note="Peptidase M48"
FT /evidence="ECO:0000259|Pfam:PF01435"
FT ACT_SITE 133
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT ACT_SITE 201
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT BINDING 132
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
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 197
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
SQ SEQUENCE 483 AA; 53857 MW; AE8C938DB1932458 CRC64;
MLKRARSLIC LCVATALSVP QVAYAELDLP DIGTAAGATL TIDQELIYGD AYMRMIRASS
PIVNDPVLNE YVDSIGHRLV SSANDVKTPF TFFMIRDRNI NAFAFFGGYV ALHTGLFLHA
HTESELASVM AHEIAHVTQR HLARRMEDEA RRSPATVAAL VGSLLLAIAS PQAGMAALTA
TTAGSMQASI NYTRSNEKEA DRFGIATLAR AKFDVNDMPR FFGRLADEYR YASKPPPMLL
THPLPEDRIT DTRERAQSYP PLRVQPSINY HLARARIVAR YAGIKSASAM DWFERTARKA
GPKIQDSFEY GKALVYLDTN KLDEAEAILD KLLKKDPNNN FYLDAASDLY IAQKRPEKAA
ELMKEVLTVK PNNPVITINY ANALLKGEKY KDSIQVLQRY THEHPNDTNG WHLLSEANIK
LGNSAEDLAA RAEILALNAQ WDKSIQLYSQ ASQLAELGSL KQARYDARID QLLVQRDRFM
ALQ
//
