ID A0A1H0R7Q1_9CLOT Unreviewed; 336 AA.
AC A0A1H0R7Q1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SAMN04488529_10367 {ECO:0000313|EMBL:SDP25524.1};
OS Clostridium gasigenes.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=94869 {ECO:0000313|EMBL:SDP25524.1, ECO:0000313|Proteomes:UP000198597};
RN [1] {ECO:0000313|EMBL:SDP25524.1, ECO:0000313|Proteomes:UP000198597}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12272 {ECO:0000313|EMBL:SDP25524.1,
RC ECO:0000313|Proteomes:UP000198597};
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; FNJM01000003; SDP25524.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0R7Q1; -.
DR STRING; 94869.SAMN04488529_10367; -.
DR Proteomes; UP000198597; 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; 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 SUPFAM; SSF50156; PDZ domain-like; 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:SDP25524.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000198597};
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 88..110
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 259..279
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 306..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 6..319
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 120..155
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF17820"
SQ SEQUENCE 336 AA; 37014 MW; D5C331860155719F CRC64;
MYIVFAMLAF SLLIIVHELG HFVMAKVNGI KVEEFAIGMG PKIFSAQGKE TKYSIGILPI
GGYVKMLGEE EEVEDNKSFS SKSPLRRISV ILAGSIMNFL LALVLFTIIL SKNGYSLPEV
GGVQENTPAY EAGLQNGDKF LNINGDKVFS KDDVAMGIVM SKGNPVDIRF ERSGEINEVT
ITPKIDDESK YLIGVSFVRI ENPTFYQGFK QSFKQTETLI VQTFKGLKML ITGKANLKTD
VGGPVTIIRL SGEAAKGGIL NLMYFTAFIS VNLAVFNLLP FPALDGGWTV ILLIELITRR
KVPDKIVATV NYIGMILLFG FMILITVKDV LFPIKF
//
