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Database: UniProt
Entry: A0A1I6JPG3_9SPHN
LinkDB: A0A1I6JPG3_9SPHN
Original site: A0A1I6JPG3_9SPHN 
ID   A0A1I6JPG3_9SPHN        Unreviewed;       376 AA.
AC   A0A1I6JPG3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN   ORFNames=SAMN05192580_0631 {ECO:0000313|EMBL:SFR80858.1};
OS   Sphingomonas jatrophae.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1166337 {ECO:0000313|EMBL:SFR80858.1, ECO:0000313|Proteomes:UP000198824};
RN   [1] {ECO:0000313|EMBL:SFR80858.1, ECO:0000313|Proteomes:UP000198824}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S5-249 {ECO:0000313|EMBL:SFR80858.1,
RC   ECO:0000313|Proteomes:UP000198824};
RA   de Groot N.N.;
RL   Submitted (OCT-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}.
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DR   EMBL; FOZG01000001; SFR80858.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6JPG3; -.
DR   STRING; 1166337.SAMN05192580_0631; -.
DR   Proteomes; UP000198824; 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; 1.
DR   PROSITE; PS50106; PDZ; 1.
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:SFR80858.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198824};
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        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        109..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   TRANSMEM        341..359
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362031"
FT   DOMAIN          131..178
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
SQ   SEQUENCE   376 AA;  40995 MW;  0848499E59169301 CRC64;
     MTQPGILWTI LAFFAVIGPL IFLHELGHYL VGRWFGVKAD AFSIGFGREI VGWTDKRGTR
     WKVAALPLGG YVKFAGDMNP ASAPTAEWLA MSPEERAGTF QAKPVWQRFL IVAAGPVTNF
     LFAIIVFMAV FAVSGEPRTP AVIAAVQPGS PAAAAGIVPG DRISMVAGQS VDRFEDISDI
     VRIRAGEAVP VDIWRNGRQI HLRMTPRVDL ERDNFGNEFR IGRIGVSPAG RTIVPLAWHE
     LPGAAVRQTV AIVRMMVDTI VQIVTGRRSV SELGGPLQIA KFSGQVATMG WFDFIIFMTM
     ISINLGFINL LPIPLLDGGH LFFYAVEAVR RRPVGPQATE WAFRSGLAVL MAFMVFVTIN
     DLGNLGLWTR LAGLIG
//
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