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Database: UniProt
Entry: F3YWA0_DESAF
LinkDB: F3YWA0_DESAF
Original site: F3YWA0_DESAF 
ID   F3YWA0_DESAF            Unreviewed;       283 AA.
AC   F3YWA0;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   RecName: Full=Protease HtpX homolog {ECO:0000256|HAMAP-Rule:MF_00188};
DE            EC=3.4.24.- {ECO:0000256|HAMAP-Rule:MF_00188};
DE   Flags: Precursor;
GN   Name=htpX {ECO:0000256|HAMAP-Rule:MF_00188};
GN   ORFNames=Desaf_0852 {ECO:0000313|EMBL:EGJ49203.1};
OS   Desulfocurvibacter africanus subsp. africanus str. Walvis Bay.
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfocurvibacter.
OX   NCBI_TaxID=690850 {ECO:0000313|EMBL:EGJ49203.1, ECO:0000313|Proteomes:UP000007844};
RN   [1] {ECO:0000313|EMBL:EGJ49203.1, ECO:0000313|Proteomes:UP000007844}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Walvis Bay {ECO:0000313|EMBL:EGJ49203.1,
RC   ECO:0000313|Proteomes:UP000007844};
RX   PubMed=21642452; DOI=10.1128/JB.05223-11;
RA   Brown S.D., Wall J.D., Kucken A.M., Gilmour C.C., Podar M., Brandt C.C.,
RA   Teshima H., Detter J.C., Han C.S., Land M.L., Lucas S., Han J.,
RA   Pennacchio L., Nolan M., Pitluck S., Woyke T., Goodwin L., Palumbo A.V.,
RA   Elias D.A.;
RT   "Genome sequence of the mercury-methylating and pleomorphic Desulfovibrio
RT   africanus Strain Walvis Bay.";
RL   J. Bacteriol. 193:4037-4038(2011).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00188};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|HAMAP-Rule:MF_00188};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00188};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00188}.
CC   -!- SIMILARITY: Belongs to the peptidase M48B family.
CC       {ECO:0000256|ARBA:ARBA00009779, ECO:0000256|HAMAP-Rule:MF_00188}.
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DR   EMBL; CP003221; EGJ49203.1; -; Genomic_DNA.
DR   RefSeq; WP_014259024.1; NC_016629.1.
DR   AlphaFoldDB; F3YWA0; -.
DR   STRING; 690850.Desaf_0852; -.
DR   KEGG; daf:Desaf_0852; -.
DR   eggNOG; COG0501; Bacteria.
DR   HOGENOM; CLU_042266_3_0_7; -.
DR   Proteomes; UP000007844; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd07336; M48B_HtpX_like; 1.
DR   Gene3D; 3.30.2010.10; Metalloproteases ('zincins'), catalytic domain; 1.
DR   HAMAP; MF_00188; Pept_M48_protease_HtpX; 1.
DR   InterPro; IPR022919; Pept_M48_protease_HtpX.
DR   InterPro; IPR001915; Peptidase_M48.
DR   PANTHER; PTHR43221; PROTEASE HTPX; 1.
DR   PANTHER; PTHR43221:SF2; PROTEASE HTPX HOMOLOG; 1.
DR   Pfam; PF01435; Peptidase_M48; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00188};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00188};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|HAMAP-Rule:MF_00188};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007844};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_00188};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_00188}.
FT   TRANSMEM        7..25
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        31..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        141..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   TRANSMEM        181..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   DOMAIN          66..279
FT                   /note="Peptidase M48"
FT                   /evidence="ECO:0000259|Pfam:PF01435"
FT   ACT_SITE        132
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         131
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         135
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
FT   BINDING         206
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00188"
SQ   SEQUENCE   283 AA;  30449 MW;  A09CEB7E6DBDD9FD CRC64;
     MSSQLKTGLL LGLLTAIVLL IGQAIGGRGG LMLAFLFAIV MNVGSYWFSD KIVLSMYRAR
     ELAPEDAPML HAMVDELAAE ARIPKPKLYV VPQESPNAFA TGRNPENAAV AVTEGIMHLL
     SPEELRGVIA HELAHVKNRD ILVQTVAAVL AGVIVMLANW VKWTAIFGFG RSDEEGGGNP
     LAALAMAIVA PIAATIIQFA ISRSREYLAD ETGARISRSP LSLAGALEKL SRGSERVPLH
     GNQATENMFI VNPFSGRSMM SLFSTHPPIE ERVARLRQMA GAR
//
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