ID SECY_ECOL6 Reviewed; 443 AA.
AC P0AGA3; P03844;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 01-MAY-2013, entry version 53.
DE RecName: Full=Protein translocase subunit SecY;
GN Name=secY; OrderedLocusNames=c4061;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P.,
RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence
RT of uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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 (By similarity).
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 (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane
CC protein (By similarity).
CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family.
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DR EMBL; AE014075; AAN82499.1; -; Genomic_DNA.
DR RefSeq; NP_755925.1; NC_004431.1.
DR ProteinModelPortal; P0AGA3; -.
DR SMR; P0AGA3; 8-442.
DR STRING; 199310.c4061; -.
DR EnsemblBacteria; AAN82499; AAN82499; c4061.
DR GeneID; 1035715; -.
DR KEGG; ecc:c4061; -.
DR PATRIC; 18285896; VBIEscCol75197_3824.
DR HOGENOM; HOG000080585; -.
DR KO; K03076; -.
DR OMA; FIMWLGE; -.
DR ProtClustDB; PRK09204; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:HAMAP.
DR GO; GO:0006605; P:protein targeting; IEA:HAMAP.
DR GO; GO:0043952; P:protein transport by the Sec complex; IEA:HAMAP.
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; IPR023201; SecY_su_dom.
DR PANTHER; PTHR10906; PTHR10906; 1.
DR Pfam; PF00344; SecY; 1.
DR PIRSF; PIRSF004557; SecY; 1.
DR SUPFAM; SSF103491; SecY; 1.
DR TIGRFAMs; TIGR00967; 3a0501s007; 1.
DR PROSITE; PS00755; SECY_1; 1.
DR PROSITE; PS00756; SECY_2; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Complete proteome; Membrane;
KW Protein transport; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1 443 Protein translocase subunit SecY.
FT /FTId=PRO_0000131723.
FT TRANSMEM 24 44 Helical; (Potential).
FT TRANSMEM 77 97 Helical; (Potential).
FT TRANSMEM 125 145 Helical; (Potential).
FT TRANSMEM 154 174 Helical; (Potential).
FT TRANSMEM 183 203 Helical; (Potential).
FT TRANSMEM 217 237 Helical; (Potential).
FT TRANSMEM 274 294 Helical; (Potential).
FT TRANSMEM 317 337 Helical; (Potential).
FT TRANSMEM 370 390 Helical; (Potential).
FT TRANSMEM 397 417 Helical; (Potential).
SQ SEQUENCE 443 AA; 48512 MW; 711CA63CD8809763 CRC64;
MAKQPGLDFQ SAKGGLGELK RRLLFVIGAL IVFRIGSFIP IPGIDAAVLA KLLEQQRGTI
IEMFNMFSGG ALSRASIFAL GIMPYISASI IIQLLTVVHP TLAEIKKEGE SGRRKISQYT
RYGTLVLAIF QSIGIATGLP NMPGMQGLVI NPGFAFYFTA VVSLVTGTMF LMWLGEQITE
RGIGNGISII IFAGIVAGLP PAIAHTIEQA RQGDLHFLVL LLVAVLVFAV TFFVVFVERG
QRRIVVNYAK RQQGRRVYAA QSTHLPLKVN MAGVIPAIFA SSIILFPATI ASWFGGGTGW
NWLTTISLYL QPGQPLYVLL YASAIIFFCF FYTALVFNPR ETADNLKKSG AFVPGIRPGE
QTAKYIDKVM TRLTLVGALY ITFICLIPEF MRDAMKVPFY FGGTSLLIVV VVIMDFMAQV
QTLMMSSQYE SALKKANLKG YGR
//
