GenomeNet

Database: UniProt
Entry: A0A150XI07_9BACT
LinkDB: A0A150XI07_9BACT
Original site: A0A150XI07_9BACT 
ID   A0A150XI07_9BACT        Unreviewed;       433 AA.
AC   A0A150XI07;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=AWW68_06085 {ECO:0000313|EMBL:KYG78334.1};
OS   Roseivirga spongicola.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Roseivirgaceae;
OC   Roseivirga.
OX   NCBI_TaxID=333140 {ECO:0000313|EMBL:KYG78334.1, ECO:0000313|Proteomes:UP000075606};
RN   [1] {ECO:0000313|EMBL:KYG78334.1, ECO:0000313|Proteomes:UP000075606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UST030701-084 {ECO:0000313|EMBL:KYG78334.1,
RC   ECO:0000313|Proteomes:UP000075606};
RA   Selvaratnam C., Thevarajoo S., Goh K.M., Ee R., Chan K.-G., Chong C.S.;
RT   "Genome sequencing of Roseivirga spongicola UST030701-084.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU362031};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the peptidase M50B family.
CC       {ECO:0000256|ARBA:ARBA00007931, ECO:0000256|RuleBase:RU362031}.
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:KYG78334.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LRPC01000001; KYG78334.1; -; Genomic_DNA.
DR   RefSeq; WP_068217883.1; NZ_LRPC01000001.1.
DR   AlphaFoldDB; A0A150XI07; -.
DR   STRING; 333140.AWW68_06085; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000075606; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR   Gene3D; 2.30.42.10; -; 2.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR004387; Pept_M50_Zn.
DR   InterPro; IPR008915; Peptidase_M50.
DR   NCBIfam; TIGR00054; RIP metalloprotease RseP; 1.
DR   PANTHER; PTHR42837:SF2; MEMBRANE METALLOPROTEASE ARASP2, CHLOROPLASTIC-RELATED; 1.
DR   PANTHER; PTHR42837; REGULATOR OF SIGMA-E PROTEASE RSEP; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 2.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU362031};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362031};
KW   Metal-binding {ECO:0000256|RuleBase:RU362031};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU362031};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KYG78334.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075606};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU362031};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU362031};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU362031}.
FT   TRANSMEM        101..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        359..381
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        410..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          10..418
FT                   /note="Peptidase M50"
FT                   /evidence="ECO:0000259|Pfam:PF02163"
SQ   SEQUENCE   433 AA;  48032 MW;  4DA15394A45801FF CRC64;
     METIVQVAQL LLALSILVGI HEGGHMLTAK MFGMKVEKFF IGFPPTLFSF KKGETEYGLG
     AIPLGGFVKI SGMIDESMDK EQMAQPPQPW EFRSKPAWQR LIVMLGGIIV NVIAGVIAFI
     ILTYNLGETY LPADLTKQEG IIAGEIAQEA GFETGDKILK VNGEDYDRVS DIWSGETLLA
     SNAYWTVERN GEVFDLPVPD GFINKLNDET FELNFIEPRR AIEVEGLQDG FDIPLEKGDR
     IVGVNGEEVL FLSDLRVKLE ALVGETATFE ILRNGQSFEY DLPVDERGQI GFVLTNPYQR
     DDYTIGEAIP RGTSKAFNAV ILNAKALGRM FGGDVNPRSL SGPIGIVNMF PKTWDWNQFW
     YTTGFISMIL AFMNLLPIPA LDGGHVMFLL YEMISGNAPS DKFLEGAQKV GMIFLLVLMV
     LVFGNDILKL FNI
//
DBGET integrated database retrieval system