ID A0A1R1SMA8_9ACTN Unreviewed; 96 AA.
AC A0A1R1SMA8;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Protein translocase subunit SecE {ECO:0000256|HAMAP-Rule:MF_00422};
GN Name=secE {ECO:0000256|HAMAP-Rule:MF_00422,
GN ECO:0000313|EMBL:OMI39426.1};
GN ORFNames=SPAR_11422 {ECO:0000313|EMBL:OMI39426.1};
OS Streptomyces sparsogenes DSM 40356.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1331668 {ECO:0000313|EMBL:OMI39426.1, ECO:0000313|Proteomes:UP000186168};
RN [1] {ECO:0000313|EMBL:OMI39426.1, ECO:0000313|Proteomes:UP000186168}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40356 {ECO:0000313|EMBL:OMI39426.1,
RC ECO:0000313|Proteomes:UP000186168};
RA Coyne S., Seebeck F.P.;
RT "Genome sequence of Streptomyces sparsogenes DSM 40356.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-
CC Rule:MF_00422}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00422};
CC Single-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_00422}.
CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. {ECO:0000256|HAMAP-
CC Rule:MF_00422}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMI39426.1}.
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DR EMBL; ASQP01000163; OMI39426.1; -; Genomic_DNA.
DR RefSeq; WP_065962948.1; NZ_ASQP01000163.1.
DR AlphaFoldDB; A0A1R1SMA8; -.
DR STRING; 67365.GCA_001704635_06768; -.
DR Proteomes; UP000186168; Unassembled WGS sequence.
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; Preprotein translocase secy subunit; 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 NCBIfam; TIGR00964; secE_bact; 1.
DR PANTHER; PTHR33910; PROTEIN TRANSLOCASE SUBUNIT SECE; 1.
DR PANTHER; PTHR33910:SF1; PROTEIN TRANSLOCASE SUBUNIT SECE; 1.
DR Pfam; PF00584; SecE; 1.
DR PROSITE; PS01067; SECE_SEC61G; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_00422};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00422};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_00422}; Reference proteome {ECO:0000313|Proteomes:UP000186168};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_00422};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_00422};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_00422};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_00422}.
FT TRANSMEM 62..83
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00422"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 96 AA; 10524 MW; B12128976A1C31E5 CRC64;
MTEALGSTAT PESGRPEDEV AAKKGRRGGK RAKKGPLGRL ALFYRQIIAE LRKVVWPTRG
QLSTYTTVVI VFVLIMIGIV TVIDFGFNHA VTYVFG
//
