ID A0A401UDB0_9BACT Unreviewed; 439 AA.
AC A0A401UDB0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SanaruYs_31610 {ECO:0000313|EMBL:GCC52921.1};
OS Chryseotalea sanaruensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae;
OC Chryseotalea.
OX NCBI_TaxID=2482724 {ECO:0000313|EMBL:GCC52921.1, ECO:0000313|Proteomes:UP000288227};
RN [1] {ECO:0000313|EMBL:GCC52921.1, ECO:0000313|Proteomes:UP000288227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ys {ECO:0000313|EMBL:GCC52921.1,
RC ECO:0000313|Proteomes:UP000288227};
RA Maejima Y., Iino T., Muraguchi Y., Fukuda K., Ohkuma M., Moriuchi R.,
RA Dohra H., Kimbara K., Shintani M.;
RT "Chryseotalea sanarue gen. nov., sp., nov., a member of the family
RT Cytophagaceae, isolated from a brackish lake in Hamamatsu Japan.";
RL Submitted (NOV-2018) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCC52921.1}.
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DR EMBL; BHXQ01000006; GCC52921.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401UDB0; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000288227; 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; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 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:GCC52921.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000288227};
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 101..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 372..398
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 210..278
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
SQ SEQUENCE 439 AA; 49044 MW; A6399B0E229B9F59 CRC64;
MEGLIMTAQI LLSLSILVAV HEMGHLLAAK YFGMRVEQFS IGFPPKIWSF TKGGTEYALS
AIPLGGYVKI SGMIDESLDL EKMKKDPEPW EFRSKPAWQR LIVMLGGIIV NVVMGIVIFI
LLTWIVGDSF IPNAAVNANG GIEARELGQE IGLKTGDKFI KINGKEFEKF EDIANPNTLL
TNNAYYTIDR NGEILDIPIP SNFIENFNEK GKILSFALPR YPPVIGKIEK NTLAERLNLQ
VGDRFVSLNG EPVTYYDDID KNKALKQDTL SFTVKRGAEL LSFNEYVGAN KGIGFYSKGF
EFEEGSTKYE FGESIAIGTE RAFGIVFTQL KAFRKLFSGE LSFRKSMSGP IGIAQAYGGD
WDWERFWRMT GLLSMVLAFM NLLPIPALDG GHVVFLTYEM VSGRKPSDKF LEVAQKAGMI
FLLGLMVFIF ANDIIKLFQ
//