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Database: UniProt
Entry: A0A1H4R3P4_9FLAO
LinkDB: A0A1H4R3P4_9FLAO
Original site: A0A1H4R3P4_9FLAO 
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
//
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