ID A0A1H4R3P4_9FLAO Unreviewed; 449 AA.
AC A0A1H4R3P4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=Zinc metalloprotease {ECO:0000256|RuleBase:RU362031};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU362031};
GN ORFNames=SAMN04489761_2526 {ECO:0000313|EMBL:SEC26549.1};
OS Tenacibaculum sp. MAR_2009_124.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Tenacibaculum.
OX NCBI_TaxID=1250059 {ECO:0000313|EMBL:SEC26549.1, ECO:0000313|Proteomes:UP000199366};
RN [1] {ECO:0000313|EMBL:SEC26549.1, ECO:0000313|Proteomes:UP000199366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mar_2009_124 {ECO:0000313|EMBL:SEC26549.1,
RC ECO:0000313|Proteomes:UP000199366};
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; FNSF01000005; SEC26549.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4R3P4; -.
DR STRING; 1250059.SAMN04489761_2526; -.
DR OrthoDB; 9782003at2; -.
DR Proteomes; UP000199366; 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; -; 2.
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; 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:SEC26549.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199366};
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 57..76
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 103..128
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 370..392
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT TRANSMEM 419..438
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362031"
FT DOMAIN 10..434
FT /note="Peptidase M50"
FT /evidence="ECO:0000259|Pfam:PF02163"
FT DOMAIN 220..286
FT /note="PDZ"
FT /evidence="ECO:0000259|Pfam:PF13180"
SQ SEQUENCE 449 AA; 50298 MW; 4956BEFA6E4C8C9E CRC64;
MEILIKASQF ILSLSLLIVL HELGHFIPAK LFKTKVEKFY LFFDYKFSLF KKKIGETVYG
IGWIPLGGYV KIAGMIDESM DKEQMKQEPK PWEFRSKPAW QRLIIMLGGV TVNFILGILI
YICLLWGYGE KFIPNSNVKD GIWVQDSLAI DLGLKTGDKI LSIDGQKIEK FGQLPIEFIN
GNNFTVERKG EAIKKEIPTD FISKLIDRGK NAGSFIRLRQ PFVIADVPKE SPNATSGLLP
KDIITAIQGE PITYFDQAKP ILEKYKGQSI TIDTKRGDNS VSIPVTISEQ ATIGVLQGRL
SAPDLERLGY YQLANKSYSF TEAIPAGTTK AWTTLTNYIK QLKKIVNPST GAYKGLGGFI
SIGSIFPSQW SWYAFWNITA FLSIMLGFMN LLPIPALDGG HVVFTLWEMI TGKKPSDKFL
EYAQVAGFVL LLALLLFANG NDIFRAIFK
//