(data stored in ACNUC7421 zone)

SWISSPROT: A0A0F6BHT5_GEOS0

ID   A0A0F6BHT5_GEOS0        Unreviewed;       430 AA.
AC   A0A0F6BHT5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   16-JAN-2019, entry version 18.
DE   RecName: Full=Protein translocase subunit SecY {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537};
GN   Name=secY {ECO:0000256|HAMAP-Rule:MF_01465};
GN   OrderedLocusNames=GY4MC1_0130 {ECO:0000313|EMBL:ADP72986.1};
OS   Geobacillus sp. (strain Y4.1MC1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72986.1, ECO:0000313|Proteomes:UP000002034};
RN   [1] {ECO:0000313|EMBL:ADP72986.1, ECO:0000313|Proteomes:UP000002034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72986.1,
RC   ECO:0000313|Proteomes:UP000002034};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA   Pitluck S., Chertkov O., Zhang X., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Jeffries C., Kyrpides N., Ivanova N.,
RA   Ovchinnikova G., Brumm P., Mead D., Woyke T.;
RT   "Complete sequence of chromosome of Geobacillus sp. Y4.1MC1.";
RL   Submitted (OCT-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The central subunit of the protein translocation channel
CC       SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These
CC       two domains form a lateral gate at the front which open onto the
CC       bilayer between TMs 2 and 7, and are clamped together by SecE at
CC       the back. The channel is closed by both a pore ring composed of
CC       hydrophobic SecY resides and a short helix (helix 2A) on the
CC       extracellular side of the membrane which forms a plug. The plug
CC       probably moves laterally to allow the channel to open. The ring
CC       and the pore may move independently. {ECO:0000256|HAMAP-
CC       Rule:MF_01465, ECO:0000256|RuleBase:RU000537}.
CC   -!- SUBUNIT: Component of the Sec protein translocase complex.
CC       Heterotrimer consisting of SecY, SecE and SecG subunits. The
CC       heterotrimers can form oligomers, although 1 heterotrimer is
CC       thought to be able to translocate proteins. Interacts with the
CC       ribosome. Interacts with SecDF, and other proteins may be
CC       involved. Interacts with SecA. {ECO:0000256|HAMAP-Rule:MF_01465}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01465}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01465}. Membrane {ECO:0000256|RuleBase:RU003484}; Multi-
CC       pass membrane protein {ECO:0000256|RuleBase:RU003484}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family.
CC       {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU004349}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01465}.
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DR   EMBL; CP002293; ADP72986.1; -; Genomic_DNA.
DR   RefSeq; WP_003247612.1; NC_014650.1.
DR   EnsemblBacteria; ADP72986; ADP72986; GY4MC1_0130.
DR   GeneID; 29237234; -.
DR   KEGG; gmc:GY4MC1_0130; -.
DR   KO; K03076; -.
DR   OMA; QTYVISQ; -.
DR   OrthoDB; 1567535at2; -.
DR   BioCyc; GSP581103:G1GOQ-157-MONOMER; -.
DR   Proteomes; UP000002034; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.3370.10; -; 1.
DR   HAMAP; MF_01465; SecY; 1.
DR   InterPro; IPR026593; SecY.
DR   InterPro; IPR002208; SecY/SEC61-alpha.
DR   InterPro; IPR030659; SecY_CS.
DR   InterPro; IPR023201; SecY_dom_sf.
DR   PANTHER; PTHR10906; PTHR10906; 1.
DR   Pfam; PF00344; SecY; 1.
DR   PIRSF; PIRSF004557; SecY; 1.
DR   SUPFAM; SSF103491; SSF103491; 1.
DR   TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR   PROSITE; PS00755; SECY_1; 1.
DR   PROSITE; PS00756; SECY_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0A0F6BHT5.
DR   SWISS-2DPAGE; A0A0F6BHT5.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002034};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01465,
KW   ECO:0000256|RuleBase:RU003484};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01465,
KW   ECO:0000256|RuleBase:RU003484};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01465,
KW   ECO:0000256|RuleBase:RU003484};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01465,
KW   ECO:0000256|RuleBase:RU003484}.
FT   TRANSMEM    109    126       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    146    166       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    178    199       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    211    234       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    271    292       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    312    329       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    363    385       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    397    413       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
SQ   SEQUENCE   430 AA;  47331 MW;  3AD87E421BD937C5 CRC64;
     MFRTISNFMR VGDIRKKIIF TLLMLIVFRI GTFIPVPNVN ADVLKVQDQM NAFGVLNIFG
     GGALQNFSIF AMGVMPYITA SIIVQLLQMD VVPKFTEWSK QGEVGRRKLA QFTRYFTVVL
     GFIQALGMSY GFNNLASGML IKNPSIPTYL LIATVLTAGT AFLMWLGELI TAKGVGNGIS
     IIIFAGIVSG IPTVLNQIYA QQFENAGDDL FLRIAMLLLL AAAVVVVIVG VIYIQQAFRK
     IPIQYAKRLE GRSPVGGHST HLPLKVNPAG VIPVIFAVSF IIAPPTIASF FGSNDVTLWI
     RNTFDYTQPV GMVIYVVLII AFTYFYAFVQ VNPEQMADNL KKQGGYIPGI RPGKNTQEYV
     TKILYRLTFV GSLFLAAVAI LPVFFVKFAN LPSSARIGGT SLLIVVGVAL ETMKQLESQL
     VKRHYKGFIK
//

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