(data stored in SCRATCH zone)

SWISSPROT: C8W405_DESAS

ID   C8W405_DESAS            Unreviewed;       421 AA.
AC   C8W405;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 61.
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=Dtox_0306 {ECO:0000313|EMBL:ACV61259.1};
OS   Desulfotomaculum acetoxidans (strain ATCC 49208 / DSM 771 / VKM
OS   B-1644) (Desulfofarcimen acetoxidans).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Peptococcaceae;
OC   Desulfofarcimen.
OX   NCBI_TaxID=485916 {ECO:0000313|EMBL:ACV61259.1, ECO:0000313|Proteomes:UP000002217};
RN   [1] {ECO:0000313|EMBL:ACV61259.1, ECO:0000313|Proteomes:UP000002217}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49208 / DSM 771 / VKM B-1644
RC   {ECO:0000313|Proteomes:UP000002217};
RX   PubMed=21304664; DOI=10.4056/sigs.39508;
RA   Spring S., Lapidus A., Schroder M., Gleim D., Sims D., Meincke L.,
RA   Glavina Del Rio T., Tice H., Copeland A., Cheng J.F., Lucas S.,
RA   Chen F., Nolan M., Bruce D., Goodwin L., Pitluck S., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K.,
RA   Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P., Saunders E.,
RA   Brettin T., Detter J.C., Goker M., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Han C.;
RT   "Complete genome sequence of Desulfotomaculum acetoxidans type strain
RT   (5575).";
RL   Stand. Genomic Sci. 1:242-253(2009).
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; CP001720; ACV61259.1; -; Genomic_DNA.
DR   RefSeq; WP_015755980.1; NC_013216.1.
DR   STRING; 485916.Dtox_0306; -.
DR   EnsemblBacteria; ACV61259; ACV61259; Dtox_0306.
DR   KEGG; dae:Dtox_0306; -.
DR   eggNOG; ENOG4105CGG; Bacteria.
DR   eggNOG; COG0201; LUCA.
DR   HOGENOM; HOG000080586; -.
DR   KO; K03076; -.
DR   OMA; QTYVISQ; -.
DR   OrthoDB; 1567535at2; -.
DR   BioCyc; DACE485916:G1GFV-321-MONOMER; -.
DR   Proteomes; UP000002217; 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; C8W405.
DR   SWISS-2DPAGE; C8W405.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002217};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01465};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01465,
KW   ECO:0000256|RuleBase:RU003484};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002217};
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     69     92       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    112    132       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    144    164       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    176    199       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    205    226       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    263    285       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    305    326       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    359    380       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
FT   TRANSMEM    386    404       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01465}.
SQ   SEQUENCE   421 AA;  45690 MW;  1038911733232377 CRC64;
     MLNGLQSAFK IGELRNKLLF TLAMLFVFRL GAHIPVPGVN PSVIADLIKS GALFGFFDVI
     SGGAFKNFSI LAMSITPYIN ASIIMQLLTV VIPHLEKLAK EGEEGRRKIT QITRYTTAVL
     AFIQGIGMVF ALRNKGILLH PNVTSYLTVA ISLTAGTVFL MWLGEQITEK GIGNGISLLI
     FAGIVSRVPA GIVNIVQYFK TGTINIFSVL GLIIIGAAVI AAIVAVQEGQ RRIPVQYAKR
     VVGRRVYGGQ TTHIPLKVNQ AGVIPVIFAS SILLFPQTVA GWFAGHAVAD WFLSVFTWGS
     FLHTVFYALL VIGFTYFYTA VIMNPIDIAD NIKKYGGFIP GLRPGRPTAE YIGRVMSRVT
     LAGAVFLAII AILPNFVLLA TRIPNIYFGG TALLIVVGVA LDTMKQVESH LLMRSYQGFI
     K
//

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