ID Q11HA7_CHESB Unreviewed; 67 AA.
AC Q11HA7;
DT 22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT 22-AUG-2006, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Protein translocase subunit SecE {ECO:0000256|HAMAP-Rule:MF_00422};
DE Flags: Precursor;
GN Name=secE {ECO:0000256|HAMAP-Rule:MF_00422};
GN OrderedLocusNames=Meso_1825 {ECO:0000313|EMBL:ABG63218.1};
OS Chelativorans sp. (strain BNC1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Chelativorans.
OX NCBI_TaxID=266779 {ECO:0000313|EMBL:ABG63218.1};
RN [1] {ECO:0000313|EMBL:ABG63218.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BNC1 {ECO:0000313|EMBL:ABG63218.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of chromosome of Chelativorans sp. BNC1.";
RL Submitted (JUN-2006) 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}.
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DR EMBL; CP000390; ABG63218.1; -; Genomic_DNA.
DR AlphaFoldDB; Q11HA7; -.
DR STRING; 266779.Meso_1825; -.
DR KEGG; mes:Meso_1825; -.
DR eggNOG; COG0690; Bacteria.
DR HOGENOM; CLU_113663_4_1_5; -.
DR OrthoDB; 9812738at2; -.
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};
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 31..51
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00422"
SQ SEQUENCE 67 AA; 7393 MW; 91ABB911524B574F CRC64;
MASRTTNPFT FLQQVRSETA KVTWPSRRET LISTVMVLAF AALAAIFFFA ADQLMAWAIE
LILGIGA
//
