GenomeNet

Database: UniProt
Entry: E1QIL8_DESB2
LinkDB: E1QIL8_DESB2
Original site: E1QIL8_DESB2 
ID   E1QIL8_DESB2            Unreviewed;       541 AA.
AC   E1QIL8;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   OrderedLocusNames=Deba_1073 {ECO:0000313|EMBL:ADK84441.1};
OS   Desulfarculus baarsii (strain ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802
OS   / 2st14).
OC   Bacteria; Thermodesulfobacteriota; Desulfarculia; Desulfarculales;
OC   Desulfarculaceae; Desulfarculus.
OX   NCBI_TaxID=644282 {ECO:0000313|EMBL:ADK84441.1, ECO:0000313|Proteomes:UP000009047};
RN   [1] {ECO:0000313|EMBL:ADK84441.1, ECO:0000313|Proteomes:UP000009047}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33931 / DSM 2075 / LMG 7858 / VKM B-1802 / 2st14
RC   {ECO:0000313|Proteomes:UP000009047};
RX   PubMed=21304732; DOI=10.4056/sigs.1243258;
RA   Sun H., Spring S., Lapidus A., Davenport K., Del Rio T.G., Tice H.,
RA   Nolan M., Copeland A., Cheng J.F., Lucas S., Tapia R., Goodwin L.,
RA   Pitluck S., Ivanova N., Pagani I., Mavromatis K., Ovchinnikova G., Pati A.,
RA   Chen A., Palaniappan K., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C.,
RA   Han C., Rohde M., Brambilla E., Goker M., Woyke T., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P., Land M.;
RT   "Complete genome sequence of Desulfarculus baarsii type strain (2st14).";
RL   Stand. Genomic Sci. 3:276-284(2010).
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC       the SecYEG preprotein conducting channel. SecDF uses the proton motive
CC       force (PMF) to complete protein translocation after the ATP-dependent
CC       function of SecA. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec protein
CC       translocation apparatus which comprises SecA, SecYEG and auxiliary
CC       proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002085; ADK84441.1; -; Genomic_DNA.
DR   RefSeq; WP_013257895.1; NC_014365.1.
DR   AlphaFoldDB; E1QIL8; -.
DR   STRING; 644282.Deba_1073; -.
DR   KEGG; dbr:Deba_1073; -.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_4_3_7; -.
DR   Proteomes; UP000009047; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:protein-transporting ATPase 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   Gene3D; 3.30.1360.200; -; 1.
DR   Gene3D; 3.30.70.3400; -; 2.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR   HAMAP; MF_01463_B; SecD_B; 1.
DR   InterPro; IPR005791; SecD.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   InterPro; IPR048631; SecD_1st.
DR   InterPro; IPR048634; SecD_SecF_C.
DR   NCBIfam; TIGR00916; 2A0604s01; 1.
DR   NCBIfam; TIGR01129; secD; 1.
DR   PANTHER; PTHR30081:SF8; PROTEIN TRANSLOCASE SUBUNIT SECF; 1.
DR   PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF21760; SecD_1st; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01463}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01463};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01463}; Reference proteome {ECO:0000313|Proteomes:UP000009047};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01463}.
FT   TRANSMEM        7..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        374..393
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        400..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        433..451
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        472..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        508..531
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          156..214
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          356..523
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   COILED          60..87
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   541 AA;  58370 MW;  11D9B14055816690 CRC64;
     MSENLTLRTA IVAVVIFIGL LFLMPNVVPK MPAWWPGFLP SDKIRLGLDL QGGMHLVLEV
     KVAQAVEASV ERTAQELERR LKSEVRATRP KAIGGNQIAI TVAGENDLAK LKDIIENQYS
     NDYEIASTKP LDRGRSEVVL RLKAEAIADI EKQASAQALE VIRNRIDQFG VAEPEIVPQE
     GGRILVQLPG VKEPKRALAL IGKTAQLEFR LVDDTIDANS ATMDSIPPGS QLLQMYRKDP
     ITGRTVKSPI VVRARRAMTG ENITDARVRP DPDYPGNYLV LVAFNSRGAA DFAEVTTKNV
     KRRLAIVLDG KVQSAPTIQE PITGGEARIT GDFGLDEAKD LAVVLRSGAL PAPIVVLEER
     TVGPSLGQDS INQGFLSMIV GFGVVVLFIL IYYKASGIIA NMALLANLVL ILGAMGLLGA
     MPEFQATLTM PGIAGIILTI GMAVDANVLI FERIREELRA GKTPAAAVEA GYGRATMTIL
     DANITTLIVA LVLLQFGTGP VRGFAVTLSL GIASSLFTAI TLTRVVFDWI LRKYQPKKLS
     I
//
DBGET integrated database retrieval system