ID A0A1H9YH62_9CLOT Unreviewed; 336 AA.
AC A0A1H9YH62;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SAMN05660297_00231 {ECO:0000313|EMBL:SES68330.1};
OS Natronincola peptidivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Natronincola.
OX NCBI_TaxID=426128 {ECO:0000313|EMBL:SES68330.1, ECO:0000313|Proteomes:UP000199568};
RN [1] {ECO:0000313|EMBL:SES68330.1, ECO:0000313|Proteomes:UP000199568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 18979 {ECO:0000313|EMBL:SES68330.1,
RC ECO:0000313|Proteomes:UP000199568};
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; FOHU01000001; SES68330.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9YH62; -.
DR STRING; 426128.SAMN05660297_00231; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000199568; 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; 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; PF13180; PDZ_2; 1.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 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:SES68330.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199568};
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 89..112
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 262..284
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 308..327
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 108..176
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 336 AA; 37259 MW; 9E005A300C75200F CRC64;
MFTALTAILV FGLLVFFHEL GHFSIAKMVG IKVHEFAIGM GPRLLKYTKG ETDYSVRMLP
IGGYVKMEGE DENSDDLRSF SNKTVGERIA VIFAGPFMNF ILAMILFAII FYNVAGTPTT
TIEEVIENSP AESVGIQKND EIISINNAAV NDWEQLVQKI NDSEGVTLKI GLVRGNEKIE
KIVAPQIEEE TNRYMIGIVP HTEKSFTLAM RGSYLQTKMI FTEMFGFFRG LLTRQTTDAE
VVGPVGIISL VGQASRDGLY NVLYLAGLIS INLGIINLLP IPALDGSRIL FLVFEFFRGK
PVDPEKEAMV HMVGLALLML LMIIITYKDI LTIFSG
//
