(data stored in SCRATCH 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   11-DEC-2019, entry version 23.
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;
OC   unclassified Geobacillus.
OX   NCBI_TaxID=581103 {ECO:0000313|EMBL:ADP72986.1};
RN   [1] {ECO:0000313|EMBL:ADP72986.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y4.1MC1 {ECO:0000313|EMBL:ADP72986.1};
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., Land M.,
RA   Hauser L., Jeffries C., Kyrpides N., Ivanova N., Ovchinnikova G., Brumm P.,
RA   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 two
CC       domains form a lateral gate at the front which open onto the bilayer
CC       between TMs 2 and 7, and are clamped together by SecE at the back. The
CC       channel is closed by both a pore ring composed of hydrophobic SecY
CC       resides and a short helix (helix 2A) on the extracellular side of the
CC       membrane which forms a plug. The plug probably moves laterally to allow
CC       the channel to open. The ring and the pore may move independently.
CC       {ECO:0000256|HAMAP-Rule:MF_01465, ECO:0000256|RuleBase:RU000537}.
CC   -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC       consisting of SecY, SecE and SecG subunits. The heterotrimers can form
CC       oligomers, although 1 heterotrimer is thought to be able to translocate
CC       proteins. Interacts with the ribosome. Interacts with SecDF, and other
CC       proteins may be involved. Interacts with SecA. {ECO:0000256|HAMAP-
CC       Rule:MF_01465}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01465}. Membrane
CC       {ECO:0000256|RuleBase:RU003484}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU003484}.
CC   -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000256|HAMAP-
CC       Rule:MF_01465, ECO:0000256|RuleBase:RU004349}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       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; FIMWLGE; -.
DR   OrthoDB; 1567535at2; -.
DR   BioCyc; GSP581103:G1GOQ-157-MONOMER; -.
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   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, ECO:0000256|RuleBase:RU003484}.
FT   TRANSMEM        109..126
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        178..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        211..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        271..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        312..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        363..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01465"
FT   TRANSMEM        397..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule: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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