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Database: UniProt
Entry: A0A1P8UR63_9RHOB
LinkDB: A0A1P8UR63_9RHOB
Original site: A0A1P8UR63_9RHOB 
ID   A0A1P8UR63_9RHOB        Unreviewed;        63 AA.
AC   A0A1P8UR63;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Protein translocase subunit SecE {ECO:0000256|HAMAP-Rule:MF_00422};
GN   Name=secE {ECO:0000256|HAMAP-Rule:MF_00422};
GN   ORFNames=Ga0080574_TMP1559 {ECO:0000313|EMBL:APZ51893.1};
OS   Salipiger abyssi.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Salipiger.
OX   NCBI_TaxID=1250539 {ECO:0000313|EMBL:APZ51893.1, ECO:0000313|Proteomes:UP000187059};
RN   [1] {ECO:0000313|EMBL:APZ51893.1, ECO:0000313|Proteomes:UP000187059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLT2014 {ECO:0000313|EMBL:APZ51893.1,
RC   ECO:0000313|Proteomes:UP000187059};
RA   Tang K.;
RT   "Deep-sea bacteria in the southern Pacific.";
RL   Submitted (APR-2016) 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; CP015093; APZ51893.1; -; Genomic_DNA.
DR   RefSeq; WP_076696787.1; NZ_JAEKIS010000033.1.
DR   AlphaFoldDB; A0A1P8UR63; -.
DR   STRING; 1250539.Ga0080574_TMP1559; -.
DR   KEGG; paby:Ga0080574_TMP1559; -.
DR   OrthoDB; 9812738at2; -.
DR   Proteomes; UP000187059; Chromosome.
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.
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:UP000187059};
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        26..51
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00422"
SQ   SEQUENCE   63 AA;  6968 MW;  CC9FD5F9A4F2283C CRC64;
     MANPIQFIQQ TRAEIGKIVW PTRREVMLTT VTVFIMAALT AAFFALVDIL IRGGLQGLLS
     MFG
//
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