SECE_STRGR
ID SECE_STRGR Reviewed; 95 AA.
AC P36690;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 2.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422};
GN Name=secE {ECO:0000255|HAMAP-Rule:MF_00422};
OS Streptomyces griseus.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=N2-3-11;
RX PubMed=8039667; DOI=10.1111/j.1574-6968.1994.tb06863.x;
RA Kuberski S., Kasberg T., Distler J.;
RT "The nusG gene of Streptomyces griseus: cloning of the gene and analysis of
RT the A-factor binding properties of the gene product.";
RL FEMS Microbiol. Lett. 119:33-39(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 10-95.
RC STRAIN=IFO 13350 / CBS 651.72;
RX PubMed=8286423;
RA Miyake K., Onaka H., Horinouchi S., Beppu T.;
RT "Organization and nucleotide sequence of the secE-nusG region of
RT Streptomyces griseus.";
RL Biochim. Biophys. Acta 1217:97-100(1994).
CC -!- FUNCTION: Essential subunit of the Sec protein translocation channel
CC SecYEG. Clamps together the 2 halves of SecY. May contact the channel
CC plug during translocation. {ECO:0000255|HAMAP-Rule:MF_00422}.
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. {ECO:0000255|HAMAP-
CC Rule:MF_00422}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00422};
CC Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_00422}.
CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000255|HAMAP-
CC Rule:MF_00422}.
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DR EMBL; X72787; CAA51295.1; -; Genomic_DNA.
DR EMBL; D17464; BAA04280.1; -; Genomic_DNA.
DR PIR; S41060; S41060.
DR AlphaFoldDB; P36690; -.
DR SMR; P36690; -.
DR STRING; 1911.GCA_001715295_02338; -.
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:0008320; F:protein transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR GO; GO:0009306; P:protein secretion; 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; 1.20.5.1030; -; 1.
DR HAMAP; MF_00422; SecE; 1.
DR InterPro; IPR005807; SecE_bac.
DR InterPro; IPR038379; SecE_sf.
DR InterPro; IPR001901; Translocase_SecE/Sec61-g.
DR PANTHER; PTHR33910; PTHR33910; 1.
DR Pfam; PF00584; SecE; 1.
DR TIGRFAMs; TIGR00964; secE_bact; 1.
DR PROSITE; PS01067; SECE_SEC61G; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..95
FT /note="Protein translocase subunit SecE"
FT /id="PRO_0000104185"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00422"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 95 AA; 10486 MW; BAE22A0C2A4B2FA5 CRC64;
MTDAVGSIDM PDAEDEAPES KKKSRKGGKR GKKGPLGRLA LFYRQIVAEL RKVVWPTRSQ
LTTYTSVVIV FVVVMIGLVT VLDIGFARVV KYVFG
