SECY_THET8
ID SECY_THET8 Reviewed; 438 AA.
AC Q5SHQ8;
DT 14-DEC-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 93.
DE RecName: Full=Protein translocase subunit SecY;
GN Name=secY; OrderedLocusNames=TTHA1672;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 3-434 OF THE SECYE COMPLEX WITH A
RP PARTIALLY OPEN LATERAL GATE, SUBUNIT, SUBCELLULAR LOCATION, AND INTERACTION
RP WITH SECA.
RX PubMed=18923527; DOI=10.1038/nature07421;
RA Tsukazaki T., Mori H., Fukai S., Ishitani R., Mori T., Dohmae N.,
RA Perederina A., Sugita Y., Vassylyev D.G., Ito K., Nureki O.;
RT "Conformational transition of Sec machinery inferred from bacterial SecYE
RT structures.";
RL Nature 455:988-991(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:18923527}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:18923527}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:18923527}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AP008226; BAD71495.1; -; Genomic_DNA.
DR RefSeq; WP_011228842.1; NC_006461.1.
DR RefSeq; YP_144938.1; NC_006461.1.
DR PDB; 2ZJS; X-ray; 3.20 A; Y=3-434.
DR PDB; 2ZQP; X-ray; 6.00 A; Y=3-434.
DR PDB; 5AWW; X-ray; 2.72 A; Y=1-438.
DR PDB; 5CH4; X-ray; 3.64 A; Y=1-435.
DR PDBsum; 2ZJS; -.
DR PDBsum; 2ZQP; -.
DR PDBsum; 5AWW; -.
DR PDBsum; 5CH4; -.
DR AlphaFoldDB; Q5SHQ8; -.
DR SMR; Q5SHQ8; -.
DR STRING; 300852.55773054; -.
DR ABCD; Q5SHQ8; 1 sequenced antibody.
DR EnsemblBacteria; BAD71495; BAD71495; BAD71495.
DR GeneID; 3169829; -.
DR KEGG; ttj:TTHA1672; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_2_0; -.
DR OMA; FAMWLGE; -.
DR PhylomeDB; Q5SHQ8; -.
DR EvolutionaryTrace; Q5SHQ8; -.
DR Proteomes; UP000000532; 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; 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..438
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000414214"
FT TOPO_DOM 1..18
FT /note="Cytoplasmic"
FT TRANSMEM 19..34
FT /note="Helical; Name=1"
FT TOPO_DOM 35..56
FT /note="Periplasmic"
FT TRANSMEM 57..87
FT /note="Discontinuously helical; Name=2"
FT INTRAMEM 57..67
FT /note="Helical; Name=Helix 2A"
FT INTRAMEM 68..71
FT INTRAMEM 72..87
FT /note="Helical; Name=Helix 2B"
FT TOPO_DOM 88..114
FT /note="Cytoplasmic"
FT TRANSMEM 115..130
FT /note="Helical; Name=3"
FT TOPO_DOM 131..157
FT /note="Periplasmic"
FT TRANSMEM 158..175
FT /note="Helical; Name=4"
FT TOPO_DOM 176..182
FT /note="Cytoplasmic"
FT TRANSMEM 183..201
FT /note="Helical; Name=5"
FT TOPO_DOM 202..214
FT /note="Periplasmic"
FT TRANSMEM 215..231
FT /note="Helical; Name=6"
FT TOPO_DOM 232..271
FT /note="Cytoplasmic"
FT TRANSMEM 272..288
FT /note="Helical; Name=7"
FT TOPO_DOM 289..303
FT /note="Periplasmic"
FT TRANSMEM 304..323
FT /note="Helical; Name=8"
FT TOPO_DOM 324..372
FT /note="Cytoplasmic"
FT TRANSMEM 373..389
FT /note="Helical; Name=9"
FT TOPO_DOM 390..392
FT /note="Periplasmic"
FT TRANSMEM 393..408
FT /note="Helical; Name=10"
FT TOPO_DOM 409..438
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT HELIX 2..10
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 12..31
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 53..56
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 57..61
FT /evidence="ECO:0007829|PDB:5AWW"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 66..69
FT /evidence="ECO:0007829|PDB:5AWW"
FT TURN 72..77
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 78..93
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:5AWW"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 108..133
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 137..140
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 151..178
FT /evidence="ECO:0007829|PDB:5AWW"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 183..193
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 196..209
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 214..236
FT /evidence="ECO:0007829|PDB:5AWW"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:5AWW"
FT STRAND 248..250
FT /evidence="ECO:0007829|PDB:5AWW"
FT STRAND 253..255
FT /evidence="ECO:0007829|PDB:5AWW"
FT STRAND 257..267
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 272..288
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 295..303
FT /evidence="ECO:0007829|PDB:5AWW"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2ZJS"
FT HELIX 309..330
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 333..342
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 354..389
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 394..396
FT /evidence="ECO:0007829|PDB:5AWW"
FT HELIX 398..423
FT /evidence="ECO:0007829|PDB:5AWW"
SQ SEQUENCE 438 AA; 48204 MW; 71BBEF926123A69E CRC64;
MLKAFWSALQ IPELRQRVLF TLLVLAAYRL GAFIPTPGVD LDKIQEFLRT AQGGVFGIIN
LFSGGNFERF SIFALGIMPY ITAAIIMQIL VTVVPALEKL SKEGEEGRRI INQYTRIGGI
ALGAFQGFFL ATAFLGAEGG RFLLPGWSPG PFFWFVVVVT QVAGIALLLW MAERITEYGI
GNGTSLIIFA GIVVEWLPQI LRTIGLIRTG EVNLVAFLFF LAFIVLAFAG MAAVQQAERR
IPVQYARKVV GRRVYGGQAT YIPIKLNAAG VIPIIFAAAI LQIPIFLAAP FQDNPVLQGI
ANFFNPTRPS GLFIEVLLVI LFTYVYTAVQ FDPKRIAESL REYGGFIPGI RPGEPTVKFL
EHIVSRLTLW GALFLGLVTL LPQIIQNLTG IHSIAFSGIG LLIVVGVALD TLRQVESQLM
LRSYEGFLSR GRLRGRNR
