SECY_AQUAE
ID SECY_AQUAE Reviewed; 429 AA.
AC O66491;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Protein translocase subunit SecY;
GN Name=secY; OrderedLocusNames=aq_079;
OS Aquifex aeolicus (strain VF5).
OC Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX NCBI_TaxID=224324;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VF5;
RX PubMed=9537320; DOI=10.1038/32831;
RA Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL Nature 392:353-358(1998).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (7.5 ANGSTROMS) OF SECYEG IN COMPLEX WITH B.SUBTILIS
RP 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 (By
CC similarity). {ECO:0000250}.
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 (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}.
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DR EMBL; AE000657; AAC06435.1; -; Genomic_DNA.
DR PIR; H70307; H70307.
DR RefSeq; NP_213051.1; NC_000918.1.
DR RefSeq; WP_010879989.1; NC_000918.1.
DR PDB; 3DL8; X-ray; 7.50 A; G/H=1-429.
DR PDBsum; 3DL8; -.
DR AlphaFoldDB; O66491; -.
DR SMR; O66491; -.
DR DIP; DIP-59810N; -.
DR IntAct; O66491; 2.
DR STRING; 224324.aq_079; -.
DR EnsemblBacteria; AAC06435; AAC06435; aq_079.
DR KEGG; aae:aq_079; -.
DR PATRIC; fig|224324.8.peg.69; -.
DR eggNOG; COG0201; Bacteria.
DR HOGENOM; CLU_030313_0_2_0; -.
DR InParanoid; O66491; -.
DR OMA; FAMWLGE; -.
DR OrthoDB; 1567535at2; -.
DR EvolutionaryTrace; O66491; -.
DR Proteomes; UP000000798; 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..429
FT /note="Protein translocase subunit SecY"
FT /id="PRO_0000131707"
FT TOPO_DOM 1..13
FT /note="Cytoplasmic"
FT TRANSMEM 14..40
FT /note="Helical; Name=1"
FT TOPO_DOM 41..64
FT /note="Periplasmic"
FT TRANSMEM 65..98
FT /note="Discontinuously helical; Name=Helix 2"
FT INTRAMEM 65..72
FT /note="Helical; Name=Helix 2A"
FT INTRAMEM 73..77
FT INTRAMEM 78..98
FT /note="Helical; Name=Helix 2B"
FT TOPO_DOM 99..111
FT /note="Cytoplasmic"
FT TRANSMEM 112..132
FT /note="Helical; Name=3"
FT TOPO_DOM 133..154
FT /note="Periplasmic"
FT TRANSMEM 155..178
FT /note="Helical; Name=4"
FT TOPO_DOM 179..181
FT /note="Cytoplasmic"
FT TRANSMEM 182..200
FT /note="Helical; Name=5"
FT TOPO_DOM 201..214
FT /note="Periplasmic"
FT TRANSMEM 215..235
FT /note="Helical; Name=6"
FT TOPO_DOM 236..267
FT /note="Cytoplasmic"
FT TRANSMEM 268..286
FT /note="Helical; Name=7"
FT TOPO_DOM 287..307
FT /note="Periplasmic"
FT TRANSMEM 308..329
FT /note="Helical; Name=8"
FT TOPO_DOM 330..360
FT /note="Cytoplasmic"
FT TRANSMEM 361..385
FT /note="Helical; Name=9"
FT TOPO_DOM 386..393
FT /note="Periplasmic"
FT TRANSMEM 394..414
FT /note="Helical; Name=10"
FT TOPO_DOM 415..429
FT /note="Cytoplasmic"
SQ SEQUENCE 429 AA; 48100 MW; 87D4FC133D037C25 CRC64;
MSEYLKALFE LKELRQKFIF TLLMFVIYRL GSHIPIPGIN PEALRDFLKA FEGSVFALYD
IFSGGNLGRL TVFALGVMPY ISASIMMQLL TVAIPSLQRL AKEEGDYGRY KINEYTKYLT
LFVATVQSLG IAFWIRGQVS PKGIPVVENP GISFILITVL TLVAGTMFLV WIADRITEKG
IGNGASLIIF AGIVANFPNA VIQFYEKVKT GDIGPLTLLL IIALIIAIIV GIVYVQEAER
RIPIQYPGRQ VGRQLYAGRK TYLPIKINPA GVIPIIFAQA LLLIPSTLLN FVQNPFIKVI
ADMFQPGAIF YNFLYVTFIV FFTYFYTAVL INPVELAENL HKAGAFIPGV RPGQDTVKYL
ERIINRLIFF GALFLSVIAL IPILISVWFN IPFYFGGTTA LIVVGVALDT FRQIETYLIQ
KKYKSYVRR
