ID A0A1T4MZF3_9GAMM Unreviewed; 453 AA.
AC A0A1T4MZF3;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=SAMN02745674_00662 {ECO:0000313|EMBL:SJZ72372.1};
OS Lysobacter spongiicola DSM 21749.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1122188 {ECO:0000313|EMBL:SJZ72372.1, ECO:0000313|Proteomes:UP000190061};
RN [1] {ECO:0000313|EMBL:SJZ72372.1, ECO:0000313|Proteomes:UP000190061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21749 {ECO:0000313|EMBL:SJZ72372.1,
RC ECO:0000313|Proteomes:UP000190061};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUXP01000001; SJZ72372.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4MZF3; -.
DR STRING; 1122188.SAMN02745674_00662; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000190061; 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; 2.
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:SJZ72372.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190061};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 98..120
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 378..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 423..444
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 11..437
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
SQ SEQUENCE 453 AA; 48519 MW; 8207236ABAD64E39 CRC64;
MTELLGSIWW LIVSLGLLVT FHEFGHYWVA RRSGVRVLKF SVGFGKPLWS RRARNGTVFQ
VAAIPLGGYV KMLDEREAPV PPEQVDLAFN RQSVWKRIAI VAAGPIANLL LCVALFWAMF
VIGRPDYAPV VGQAEGIAAE AGLQRGDTIL AVGERETPTW SEVQLAIIPA ALDRADTRLH
IRTADGEATT RTLALSNLPA QIDERRAVNA AGLVPRHLLA PALVGRVAPD TAAWGVLAEG
DIITAVDGRP VQAWTDIGPA VEAWGEEGGT GMVEVLRDGE RLALELAPTR IQPDDGEPYW
ALGITSARAS LPEMDAELRY GPAAALPAAL AETAHQGREL FAMIGRAFTG RVEVENTVAG
PVTIARAANA YAGQGAAWYL SLLAMLSLSL GILNLLPIPI LDGGHLLYYL IELVKGSPVS
ERAMAAGQYV GLALIVGLMG LAFYNDIINN LVR
//
