SECG_PYRCJ
ID SECG_PYRCJ Reviewed; 58 AA.
AC A3MT10;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Preprotein translocase subunit SecG {ECO:0000255|HAMAP-Rule:MF_00751};
DE AltName: Full=Protein transport protein Sec61 subunit beta homolog {ECO:0000255|HAMAP-Rule:MF_00751};
GN Name=secG {ECO:0000255|HAMAP-Rule:MF_00751}; OrderedLocusNames=Pcal_0342;
OS Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=410359;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21063 / JCM 11548 / VA1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Involved in protein export. The function of the beta subunit
CC is unknown, but it may be involved in stabilization of the trimeric
CC complex. {ECO:0000255|HAMAP-Rule:MF_00751}.
CC -!- SUBUNIT: Component of the protein translocase complex. Heterotrimer
CC consisting of alpha (SecY), beta (SecG) and gamma (SecE) subunits. Can
CC form oligomers of the heterotrimer. {ECO:0000255|HAMAP-Rule:MF_00751}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00751};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00751}.
CC -!- SIMILARITY: Belongs to the SEC61-beta family. {ECO:0000255|HAMAP-
CC Rule:MF_00751}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000561; ABO07777.1; -; Genomic_DNA.
DR AlphaFoldDB; A3MT10; -.
DR SMR; A3MT10; -.
DR STRING; 410359.Pcal_0342; -.
DR EnsemblBacteria; ABO07777; ABO07777; Pcal_0342.
DR KEGG; pcl:Pcal_0342; -.
DR eggNOG; arCOG02957; Archaea.
DR HOGENOM; CLU_208205_2_1_2; -.
DR Proteomes; UP000001431; 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 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 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..58
FT /note="Preprotein translocase subunit SecG"
FT /id="PRO_1000046581"
FT TOPO_DOM 1..33
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT TRANSMEM 34..55
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
FT TOPO_DOM 56..58
FT /note="Extracellular"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00751"
SQ SEQUENCE 58 AA; 6242 MW; B1CBB424F57AE787 CRC64;
MARRRKYEGL NPFVAAGLIK FSEEGELEKI KLSPKAAIAI SLAIIAAILA LNLLLPPP