ID A0A1Y1RVE1_9SPIO Unreviewed; 456 AA.
AC A0A1Y1RVE1;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-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=B4O97_14660 {ECO:0000313|EMBL:ORC33900.1};
OS Marispirochaeta aestuarii.
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Marispirochaeta.
OX NCBI_TaxID=1963862 {ECO:0000313|EMBL:ORC33900.1, ECO:0000313|Proteomes:UP000192343};
RN [1] {ECO:0000313|EMBL:ORC33900.1, ECO:0000313|Proteomes:UP000192343}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JC444 {ECO:0000313|EMBL:ORC33900.1,
RC ECO:0000313|Proteomes:UP000192343};
RA Shivani Y., Subhash Y., Sasikala C., Ramana C.;
RT "Draft Genome sequence of Marispirochaeta sp. strain JC444.";
RL Submitted (MAR-2017) 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:ORC33900.1}.
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DR EMBL; MWQY01000017; ORC33900.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y1RVE1; -.
DR STRING; 1963862.B4O97_14660; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000192343; 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; 2.
DR CDD; cd06163; S2P-M50_PDZ_RseP-like; 1.
DR Gene3D; 2.30.42.10; -; 2.
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; 2.
DR Pfam; PF02163; Peptidase_M50; 1.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; PDZ domain-like; 2.
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:ORC33900.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000192343};
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..125
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 429..453
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 190..282
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
SQ SEQUENCE 456 AA; 49837 MW; 5A611A793625157B CRC64;
MLFTIVAGLI GLGIVIFVHE TGHFLAAKAM GIEVEAFSLG WGNPLVRFSF RGTEYRISSL
PIGGYCKLKG EQNLQPGESP DSARITTEEG SLFSVAPWRR IITFLAGPVS NLLFSVLILS
LIWGIGYSIQ TFGNRIILVS EYGSVASGDS RYPADIAGLE TGDRILSIDG EKVSYYRDIQ
ELISIRADKT TDLSVERNGE VLNLSITPML NPQTGGGIIG VSPWIEAVVE EVSPGSPASA
AGIRPGDRIV AVQGHPVSNH LDFLQALQGH PLRFGLTVER NGERLELRMV PDYDENGNPL
LGISYKSITS KQQASSVIDA FSRGIGESFS ILGLSIRSFA LLFKGIDLQQ AVSGPIRITY
MVGQVASSGF SDGIMTGLIS LFRFLSFLSI ALFVMNLLPI PALDGGLIVI TLFEMIRRKR
ISPKVFNRYQ VFGFIFIMTL LVFTTFNDIF YFFTNH
//