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Database: UniProt
Entry: Q1ZJI9_PHOAS
LinkDB: Q1ZJI9_PHOAS
Original site: Q1ZJI9_PHOAS 
ID   Q1ZJI9_PHOAS            Unreviewed;       485 AA.
AC   Q1ZJI9;
DT   02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT   02-MAY-2006, sequence version 1.
DT   24-JAN-2024, entry version 81.
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=VAS14_00483 {ECO:0000313|EMBL:EAS62358.1};
OS   Photobacterium angustum (strain S14 / CCUG 15956) (Vibrio sp. (strain S14 /
OS   CCUG 15956)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=314292 {ECO:0000313|EMBL:EAS62358.1, ECO:0000313|Proteomes:UP000001603};
RN   [1] {ECO:0000313|EMBL:EAS62358.1, ECO:0000313|Proteomes:UP000001603}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S14 {ECO:0000313|EMBL:EAS62358.1,
RC   ECO:0000313|Proteomes:UP000001603};
RX   PubMed=19805210; DOI=10.1073/pnas.0903507106;
RA   Lauro F.M., McDougald D., Thomas T., Williams T.J., Egan S., Rice S.,
RA   DeMaere M.Z., Ting L., Ertan H., Johnson J., Ferriera S., Lapidus A.,
RA   Anderson I., Kyrpides N., Munk A.C., Detter C., Han C.S., Brown M.V.,
RA   Robb F.T., Kjelleberg S., Cavicchioli R.;
RT   "The genomic basis of trophic strategy in marine bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:15527-15533(2009).
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:EAS62358.1}.
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DR   EMBL; AAOJ01000023; EAS62358.1; -; Genomic_DNA.
DR   RefSeq; WP_005363517.1; NZ_AAOJ01000023.1.
DR   AlphaFoldDB; Q1ZJI9; -.
DR   MEROPS; M48.023; -.
DR   HOGENOM; CLU_030556_1_1_6; -.
DR   OrthoDB; 9810445at2; -.
DR   Proteomes; UP000001603; 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   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; METALLOENDOPEPTIDASE OMA1; 1.
DR   PANTHER; PTHR22726:SF1; METALLOENDOPEPTIDASE OMA1, MITOCHONDRIAL; 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|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..485
FT                   /note="Putative beta-barrel assembly-enhancing protease"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT                   /id="PRO_5009019002"
FT   DOMAIN          71..253
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   ACT_SITE        135
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT   ACT_SITE        203
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT   BINDING         134
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT   BINDING         138
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
FT   BINDING         199
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00997"
SQ   SEQUENCE   485 AA;  54129 MW;  2D5A58D747D06C25 CRC64;
     MFRFANAPTY LLLSALLSSS IPAIASDDNR LPEMGTTASS TLTIDKEREY GDAYMRVIRA
     SQPVISDPLL SDYVQSLGHK LVANAEGVRT PFYFFLIQNY EINAFAFFGG HVALHSGLFL
     HAQSESELAS VLAHEIAHVT QRHLARKMEA DAKNSPLTVA ALVGSLLLTV AAPEAGIAAI
     HATTAANIQG QINFTRSNEK EADSIGIKTL AKAGFDAHAM PRFFERLAEQ YRYTSKLPAM
     LLTHPLPESR VTDSRMRARN YPTVVLPPSE RYLLARSRVV ARNAGFSETS SLNWLNRELK
     KAAPNRRKEL NYGKALVYID NAKYQQAHQL LDPLIAGEPD NMFYIDAATD LDLNQKQYQR
     AISRLVNAQK NNPDSSVLRI NLANAYLEAG KYQQSIKILN RYTYDHPDDT NGWALLAKSY
     AKLGNRAAEL ASFGELLALR AQWDRAINNY MQAAQMAKLG SMAQARYDAR IDQLRFQRQK
     FKALQ
//
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