ID A0A1I5M9R3_9BACT Unreviewed; 456 AA.
AC A0A1I5M9R3;
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=SAMN04487852_11468 {ECO:0000313|EMBL:SFP06279.1};
OS Prevotella sp. tf2-5.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=1761889 {ECO:0000313|EMBL:SFP06279.1, ECO:0000313|Proteomes:UP000198673};
RN [1] {ECO:0000313|EMBL:SFP06279.1, ECO:0000313|Proteomes:UP000198673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TF2-5 {ECO:0000313|EMBL:SFP06279.1,
RC ECO:0000313|Proteomes:UP000198673};
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; FOWK01000014; SFP06279.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5M9R3; -.
DR STRING; 1761889.SAMN04487852_11468; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000198673; 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:SFP06279.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198673};
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 106..131
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 386..413
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 425..446
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 225..255
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 456 AA; 51283 MW; 80F91376542EE22D CRC64;
MEVFLIRVLQ FILAISLLVL LHEGGHFFFA KLFGVRVEKF YIFFDWKFSL FKFKPKNSDT
EYGVGWLPLG GYCKIAGMID ESFDTEQMKK PAQPWEFRTK PAWQRLLIMI GGVLVNFLLA
LFIYSMILFY WGDTYIPVKD MTLGMKFNQE AKSYGFKDGD ILIGTETKAF KDFSADLYRD
ISEAKRVDII RNGKKMSINL PGELNLLGML KADPAFVRPL IPAKVDSVVP GTPAEKIGIK
AGDHILALNG SPVDSYNEFI DLLGRRQDLL DTAASPADSL KARTVTIVFG HESKKDTASV
ILTPDLKLGF VVSTIAGLYK PVTKEYGFLE SIPAGIKYGC DVLGSYVGDM KYVFTADGAK
SLGGFGAIGS LFPPMWDWYM FWKMTAFLSI ILAFMNILPI PALDGGHVLF LLYEMITRRK
PSEEFMIRAE YVGFGILILL MVFANLNDIL RWLGYL
//
