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Database: UniProt
Entry: A0A1X4NIX0_9RHOB
LinkDB: A0A1X4NIX0_9RHOB
Original site: A0A1X4NIX0_9RHOB 
ID   A0A1X4NIX0_9RHOB        Unreviewed;       447 AA.
AC   A0A1X4NIX0;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=MGEO_14170 {ECO:0000313|EMBL:OSQ48970.1};
OS   Marivita geojedonensis.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Marivita.
OX   NCBI_TaxID=1123756 {ECO:0000313|EMBL:OSQ48970.1, ECO:0000313|Proteomes:UP000193926};
RN   [1] {ECO:0000313|EMBL:OSQ48970.1, ECO:0000313|Proteomes:UP000193926}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DPG-138 {ECO:0000313|EMBL:OSQ48970.1,
RC   ECO:0000313|Proteomes:UP000193926};
RA   Lai Q., Shao Z.;
RT   "The draft genome sequence of Marivita geojedonensis KCTC 23882.";
RL   Submitted (MAR-2014) 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:OSQ48970.1}.
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DR   EMBL; JFKC01000015; OSQ48970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X4NIX0; -.
DR   STRING; 1123756.MGEO_14170; -.
DR   OrthoDB; 9782003at2; -.
DR   Proteomes; UP000193926; 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; cd00989; PDZ_metalloprotease; 1.
DR   CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
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; PF17820; PDZ_6; 1.
DR   Pfam; PF02163; Peptidase_M50; 1.
DR   SMART; SM00228; PDZ; 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:OSQ48970.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000193926};
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        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        113..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        376..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        420..440
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          206..276
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|SMART:SM00228"
SQ   SEQUENCE   447 AA;  48058 MW;  185DCF509FA09933 CRC64;
     MDIAALLPQF GSVIWTLFAF VIALSIIVAI HEYGHYIVGR WSGIDADVFS LGFGPVLFSR
     VDKRGTKWQF ALLPFGGYVK FKGDGNASGG KDEDVMSRLS EAEQRRTMNG APLWARAATV
     AAGPAFNFAL SILIFTGVFM FQGEVTEPVK VGELRAVPSQ NELQVGDELV AIEGVALPPF
     SESDSFQSFL EGLPQQEHLA YTVKRNGNEL VVEGPYVYPP VATQIIPRSA ADDAGFRSGD
     IITSVDGQTI YAFDQLREAV EGSGGNTLRL DVWREGEIRT LELTPRRTDE PQPDGTFKTA
     YRIGLVGGMF FEPATEFVGP VSAIVSGVEQ TGRIIDGSLS GLWYMITGAI STCNLSGPIG
     IAETSGSMAS QGTASFIWFI AVLSTAVGLL NLFPIPVLDG GHLVFHAYEA VTGRPPSDKA
     LRVLMAIGLT LLLSLMLFAL SNDLFCP
//
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