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Database: UniProt
Entry: A0A430FD98_9BIFI
LinkDB: A0A430FD98_9BIFI
Original site: A0A430FD98_9BIFI 
ID   A0A430FD98_9BIFI        Unreviewed;        75 AA.
AC   A0A430FD98;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   13-SEP-2023, entry version 13.
DE   RecName: Full=Protein translocase subunit SecE {ECO:0000256|HAMAP-Rule:MF_00422};
GN   Name=secE {ECO:0000256|HAMAP-Rule:MF_00422};
GN   ORFNames=D2E25_1990 {ECO:0000313|EMBL:RSX50797.1};
OS   Bifidobacterium goeldii.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=2306975 {ECO:0000313|EMBL:RSX50797.1, ECO:0000313|Proteomes:UP000287533};
RN   [1] {ECO:0000313|EMBL:RSX50797.1, ECO:0000313|Proteomes:UP000287533}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2034B {ECO:0000313|EMBL:RSX50797.1,
RC   ECO:0000313|Proteomes:UP000287533};
RA   Lugli G.A., Duranti S., Milani C.;
RT   "Characterization of the phylogenetic diversity of five novel species
RT   belonging to the genus Bifidobacterium.";
RL   Submitted (SEP-2018) 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:RSX50797.1}.
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DR   EMBL; QXGL01000012; RSX50797.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A430FD98; -.
DR   OrthoDB; 9805743at2; -.
DR   Proteomes; UP000287533; 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   Pfam; PF00584; SecE; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-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:UP000287533};
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        41..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00422"
SQ   SEQUENCE   75 AA;  8449 MW;  39303E81709AD611 CRC64;
     MAKASNTEKA VKPNVFMRIG LFIKQIIDEL RKVVTPSAKE LFFWSLAVFI FVLLLMALVT
     GMDFGLGKLV LWVFG
//
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