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Database: UniProt
Entry: E3GFZ5_EUBLK
LinkDB: E3GFZ5_EUBLK
Original site: E3GFZ5_EUBLK 
ID   E3GFZ5_EUBLK            Unreviewed;       419 AA.
AC   E3GFZ5;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   27-SEP-2017, entry version 47.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   OrderedLocusNames=ELI_3520 {ECO:0000313|EMBL:ADO38479.1};
OS   Eubacterium limosum (strain KIST612).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Eubacteriaceae;
OC   Eubacterium.
OX   NCBI_TaxID=903814 {ECO:0000313|EMBL:ADO38479.1, ECO:0000313|Proteomes:UP000006873};
RN   [1] {ECO:0000313|Proteomes:UP000006873}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KIST612 {ECO:0000313|Proteomes:UP000006873};
RA   Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H.,
RA   Chang I.S., Choi I.-G.;
RT   "The genome sequence of Eubacterium limosum (strain KIST612).";
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=KIST612;
RA   Roh H., Ko H.-J., Kim D., Choi D.G., Park S., Kim S., Kim K.H.,
RA   Chang I.S., Choi I.-G.;
RL   Submitted (SEP-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. SecDF uses the
CC       proton motive force (PMF) to complete protein translocation after
CC       the ATP-dependent function of SecA. {ECO:0000256|HAMAP-
CC       Rule:MF_01463, ECO:0000256|SAAS:SAAS00541769}.
CC   -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec
CC       protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP002273; ADO38479.1; -; Genomic_DNA.
DR   RefSeq; WP_013381786.1; NC_014624.2.
DR   STRING; 903814.ELI_3520; -.
DR   EnsemblBacteria; ADO38479; ADO38479; ELI_3520.
DR   KEGG; elm:ELI_3520; -.
DR   eggNOG; ENOG4105C3D; Bacteria.
DR   eggNOG; COG0342; LUCA.
DR   HOGENOM; HOG000018636; -.
DR   KO; K03072; -.
DR   OMA; SAHLQMM; -.
DR   OrthoDB; POG091H02C5; -.
DR   Proteomes; UP000006873; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; 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   HAMAP; MF_01463_B; SecD_B; 1.
DR   InterPro; IPR001036; Acrflvin-R.
DR   InterPro; IPR005791; SecD.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006873};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006873};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM     12     31       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    255    272       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    279    301       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    307    329       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    350    372       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    378    397       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   419 AA;  44356 MW;  64AC39A215449863 CRC64;
     MKEKVNTKKT ITLVIFIAIL AFCGYTLFHG LSVGIYDIGN IGDHVHYGLD LTGGVNVVLQ
     AEATDDSGIT SEKMDSTVAA IKKRVDSMGV SEAQVSKQGE DRIRVSIPSV QDQQQALDMI
     GKTAQLEFVG PDGEVILTGK DVVDSKAVQQ KSSSGLEEAV VTLKFNDEGT QLFADATQKY
     LNQQISIKLD DEVISSPKVN VAITNGEAVI EGMADMEEAG NLAELIRGGA LPVKLSPIEV
     TTIGPTLGQD SLNQSLIAGA IGIAAVLLFM LVMYRGLGFI ADLALIIYIM LDLILMVFAN
     VTLTLPGIAG IILSVGMAVD ANVIIFERIK DESRSGKSIN AAIDAGFKRA MGTIIDSNVT
     TLIAGFVLFF MGSGSVQGFA VTLILGIIVS LLTAVIITKH LTKLVIGTHL FGSGKFYGI
//
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