SECY_THEMA
ID SECY_THEMA Reviewed; 431 AA.
AC Q9X1I9;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Protein translocase subunit SecY;
GN Name=secY; OrderedLocusNames=TM_1480;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (4.50 ANGSTROMS) OF SECYEG IN COMPLEX WITH SECA.
RX PubMed=18923516; DOI=10.1038/nature07335;
RA Zimmer J., Nam Y., Rapoport T.A.;
RT "Structure of a complex of the ATPase SecA and the protein-translocation
RT channel.";
RL Nature 455:936-943(2008).
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 -!- 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.
CC {ECO:0000269|PubMed:18923516}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36546.1; -; Genomic_DNA.
DR PIR; H72247; H72247.
DR RefSeq; NP_229280.1; NC_000853.1.
DR RefSeq; WP_004081795.1; NZ_CP011107.1.
DR PDB; 3DIN; X-ray; 4.50 A; C/F=1-431.
DR PDBsum; 3DIN; -.
DR AlphaFoldDB; Q9X1I9; -.
DR SMR; Q9X1I9; -.
DR DIP; DIP-59807N; -.
DR IntAct; Q9X1I9; 3.
DR STRING; 243274.THEMA_06900; -.
DR TCDB; 3.A.5.1.4; the general secretory pathway (sec) family.
DR EnsemblBacteria; AAD36546; AAD36546; TM_1480.
DR KEGG; tma:TM1480; -.
DR eggNOG; COG0201; Bacteria.
DR InParanoid; Q9X1I9; -.
DR OMA; FAMWLGE; -.
DR OrthoDB; 1567535at2; -.
DR EvolutionaryTrace; Q9X1I9; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IBA:GO_Central.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0005048; F:signal sequence binding; IBA:GO_Central.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..431
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000414213"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT TRANSMEM 18..32
FT /note="Helical; Name=Helix 1"
FT TOPO_DOM 33..73
FT /note="Periplasmic"
FT TRANSMEM 74..95
FT /note="Discontinuously helical; Name=Helix 2"
FT INTRAMEM 74..77
FT /note="Helical; Name=Helix 2A"
FT INTRAMEM 78..84
FT INTRAMEM 85..95
FT /note="Helical; Name=Helix 2B"
FT TOPO_DOM 96..120
FT /note="Cytoplasmic"
FT TRANSMEM 121..133
FT /note="Helical; Name=Helix 3"
FT TOPO_DOM 134..161
FT /note="Periplasmic"
FT TRANSMEM 162..178
FT /note="Helical; Name=Helix 4"
FT TOPO_DOM 179..182
FT /note="Cytoplasmic"
FT TRANSMEM 183..198
FT /note="Helical; Name=Helix 5"
FT TOPO_DOM 199..213
FT /note="Periplasmic"
FT TRANSMEM 214..226
FT /note="Helical; Name=Helix 6"
FT TOPO_DOM 227..270
FT /note="Cytoplasmic"
FT TRANSMEM 271..283
FT /note="Helical; Name=Helix 7"
FT TOPO_DOM 284..302
FT /note="Periplasmic"
FT TRANSMEM 303..315
FT /note="Helical; Name=Helix 8"
FT TOPO_DOM 316..367
FT /note="Cytoplasmic"
FT TRANSMEM 368..382
FT /note="Helical; Name=Helix 9"
FT TOPO_DOM 383..389
FT /note="Periplasmic"
FT TRANSMEM 390..403
FT /note="Helical; Name=Helix 10"
FT TOPO_DOM 404..431
FT /note="Cytoplasmic"
SQ SEQUENCE 431 AA; 48170 MW; 0FFDBBAD1F8F0B61 CRC64;
MWQAFKNAFK IPELRDRIIF TFLALIVFRM GIYIPVPGLN LEAWGEIFRR IAETAGVAGI
LSFYDVFTGG ALSRFSVFTM SVTPYITASI ILQLLASVMP SLKEMLREGE EGRKKFAKYT
RRLTLLIGGF QAFFVSFSLA RSNPDMVAPG VNVLQFTVLS TMSMLAGTMF LLWLGERITE
KGIGNGISIL IFAGIVARYP SYIRQAYLGG LNLLEWIFLI AVALITIFGI ILVQQAERRI
TIQYARRVTG RRVYGGASTY LPIKVNQGGV IPIIFASAIV SIPSAIASIT NNETLKNLFR
AGGFLYLLIY GLLVFFFTYF YSVVIFDPRE ISENIRKYGG YIPGLRPGRS TEQYLHRVLN
RVTFIGAVFL VVIALLPYLV QGAIKVNVWI GGTSALIAVG VALDIIQQME THMVMRHYEG
FIKKGKIRGR R
