SECG_METJA
ID SECG_METJA Reviewed; 53 AA.
AC P60460;
DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot.
DT 16-FEB-2004, sequence version 1.
DT 25-MAY-2022, entry version 87.
DE RecName: Full=Preprotein translocase subunit SecG;
DE AltName: Full=Protein transport protein Sec61 subunit beta homolog;
GN Name=secG; OrderedLocusNames=MJ0912.1;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 21-52 IN COMPLEX WITH SECY AND
RP SECE.
RX PubMed=14661030; DOI=10.1038/nature02218;
RA Van den Berg B., Clemons W.M. Jr., Collinson I., Modis Y., Hartmann E.,
RA Harrison S.C., Rapoport T.A.;
RT "X-ray structure of a protein-conducting channel.";
RL Nature 427:36-44(2004).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS).
RX PubMed=17531810; DOI=10.1016/j.molcel.2007.05.002;
RA Li W., Schulman S., Boyd D., Erlandson K., Beckwith J., Rapoport T.A.;
RT "The plug domain of the SecY protein stabilizes the closed state of the
RT translocation channel and maintains a membrane seal.";
RL Mol. Cell 26:511-521(2007).
RN [4]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 21-52 DOCKED ONTO
RP E.COLI RIBOSOMES.
RX PubMed=18158904; DOI=10.1016/j.molcel.2007.10.034;
RA Menetret J.F., Schaletzky J., Clemons W.M. Jr., Osborne A.R.,
RA Skanland S.S., Denison C., Gygi S.P., Kirkpatrick D.S., Park E.,
RA Ludtke S.J., Rapoport T.A., Akey C.W.;
RT "Ribosome binding of a single copy of the SecY complex: implications for
RT protein translocation.";
RL Mol. Cell 28:1083-1092(2007).
RN [5]
RP STRUCTURE BY ELECTRON MICROSCOPY (8.7 ANGSTROMS) OF 21-52 DOCKED ONTO DOG
RP RIBOSOMES.
RX PubMed=18611385; DOI=10.1016/j.str.2008.05.003;
RA Menetret J.F., Hegde R.S., Aguiar M., Gygi S.P., Park E., Rapoport T.A.,
RA Akey C.W.;
RT "Single copies of Sec61 and TRAP associate with a nontranslating mammalian
RT ribosome.";
RL Structure 16:1126-1137(2008).
RN [6]
RP STRUCTURE BY ELECTRON MICROSCOPY DOCKED ONTO E.COLI RIBOSOMES.
RX PubMed=19913480; DOI=10.1016/j.str.2009.09.010;
RA Gumbart J., Trabuco L.G., Schreiner E., Villa E., Schulten K.;
RT "Regulation of the protein-conducting channel by a bound ribosome.";
RL Structure 17:1453-1464(2009).
CC -!- FUNCTION: Subunit of the protein translocation channel SecYEG. The
CC function of the beta subunit is unknown, but it may be involved in
CC stabilization of the trimeric complex.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. The
CC heterotrimers can form oligomers, although 1 heterotrimer is thought to
CC be able to translocate proteins. Interacts with the ribosome. May
CC interact with SecDF, and other proteins may be involved.
CC {ECO:0000269|PubMed:14661030}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC -!- SIMILARITY: Belongs to the SEC61-beta family. {ECO:0000305}.
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DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; WP_064496662.1; NC_000909.1.
DR PDB; 1RH5; X-ray; 3.20 A; C=1-53.
DR PDB; 1RHZ; X-ray; 3.50 A; C=1-53.
DR PDB; 2YXQ; X-ray; 3.50 A; C=1-53.
DR PDB; 2YXR; X-ray; 3.60 A; C=1-53.
DR PDB; 3BO0; EM; 9.60 A; C=21-52.
DR PDB; 3BO1; EM; 9.60 A; C=21-52.
DR PDB; 3DKN; EM; 8.70 A; C=21-52.
DR PDB; 4V4N; EM; 9.00 A; A8=1-52.
DR PDB; 4V7I; EM; 9.60 A; AC=1-53.
DR PDBsum; 1RH5; -.
DR PDBsum; 1RHZ; -.
DR PDBsum; 2YXQ; -.
DR PDBsum; 2YXR; -.
DR PDBsum; 3BO0; -.
DR PDBsum; 3BO1; -.
DR PDBsum; 3DKN; -.
DR PDBsum; 4V4N; -.
DR PDBsum; 4V7I; -.
DR AlphaFoldDB; P60460; -.
DR SMR; P60460; -.
DR IntAct; P60460; 2.
DR MINT; P60460; -.
DR TCDB; 3.A.5.7.4; the general secretory pathway (sec) family.
DR GeneID; 27929979; -.
DR OMA; GLIRYMD; -.
DR OrthoDB; 127915at2157; -.
DR EvolutionaryTrace; P60460; -.
DR Proteomes; UP000000805; 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:0015031; P:protein transport; IEA:UniProtKB-UniRule.
DR DisProt; DP00964; -.
DR HAMAP; MF_00751; SecG; 1.
DR InterPro; IPR023531; Preprot_translocase_SecG.
DR InterPro; IPR016482; SecG/Sec61-beta/Sbh.
DR Pfam; PF03911; Sec61_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..53
FT /note="Preprotein translocase subunit SecG"
FT /id="PRO_0000157268"
FT TOPO_DOM 1..30
FT /note="Cytoplasmic"
FT TRANSMEM 31..49
FT /note="Helical"
FT TOPO_DOM 50..53
FT /note="Extracellular"
FT HELIX 30..49
FT /evidence="ECO:0007829|PDB:1RH5"
SQ SEQUENCE 53 AA; 5959 MW; D2D5DD22331BE2AF CRC64;
MSKREETGLA TSAGLIRYMD ETFSKIRVKP EHVIGVTVAF VIIEAILTYG RFL
