ID A0A1M4W606_9FIRM Unreviewed; 345 AA.
AC A0A1M4W606;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN02745190_01112 {ECO:0000313|EMBL:SHE76637.1};
OS Schwartzia succinivorans DSM 10502.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Schwartzia.
OX NCBI_TaxID=1123243 {ECO:0000313|EMBL:SHE76637.1, ECO:0000313|Proteomes:UP000184404};
RN [1] {ECO:0000313|EMBL:SHE76637.1, ECO:0000313|Proteomes:UP000184404}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10502 {ECO:0000313|EMBL:SHE76637.1,
RC ECO:0000313|Proteomes:UP000184404};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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; FQUG01000004; SHE76637.1; -; Genomic_DNA.
DR RefSeq; WP_072935196.1; NZ_FQUG01000004.1.
DR AlphaFoldDB; A0A1M4W606; -.
DR STRING; 1123243.SAMN02745190_01112; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000184404; 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 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:SHE76637.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184404};
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 95..117
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 265..287
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 314..333
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 9..329
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 130..186
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
SQ SEQUENCE 345 AA; 37731 MW; 6A0DB1F57C9B1E88 CRC64;
MVYTIAASIL VFGFLVLFHE LGHFALAKWT GMRVDEFAIG FGPRIWSKKY GETEYSIRCI
PLGGFNDIAG MNPADNDAGD RGYCAKPVWK RMLTILAGPG MNLILPIFIF AVIFFSVGVS
TPSTRPELGD ILPDKPAAMS GLKKGDTIRR INDVEIHEWS DIVREILANG QKSMTVDYVR
DGKEYQTTMV PEYDKQNNRP VVGIMSSSDI RQPGLFEAVY LAVYKNGVII YEMLNGLVKI
FSGSAAAELA GPIGVMQMTG EVAQIGFVPL LHFAAVLSLN LGIINLLPVP ALDGGHFVTL
IIEALRGKPL GDKALHYTQM VGITLLIALM LFATKNDIVR IFFAG
//
