ID   SECD_DEHMV              Reviewed;         449 AA.
AC   D2BGI6;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   09-FEB-2010, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=DhcVS_275;
OS   Dehalococcoides mccartyi (strain VS).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=311424;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VS;
RX   PubMed=19893622; DOI=10.1371/journal.pgen.1000714;
RA   McMurdie P.J., Behrens S.F., Muller J.A., Goke J., Ritalahti K.M.,
RA   Wagner R., Goltsman E., Lapidus A., Holmes S., Loffler F.E., Spormann A.M.;
RT   "Localized plasticity in the streamlined genomes of vinyl chloride
RT   respiring Dehalococcoides.";
RL   PLoS Genet. 5:E1000714-E1000714(2009).
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:0000255|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:0000255|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01463};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP001827; ACZ61436.1; -; Genomic_DNA.
DR   RefSeq; WP_012881612.1; NC_013552.1.
DR   AlphaFoldDB; D2BGI6; -.
DR   SMR; D2BGI6; -.
DR   STRING; 311424.DhcVS_275; -.
DR   EnsemblBacteria; ACZ61436; ACZ61436; DhcVS_275.
DR   KEGG; dev:DhcVS_275; -.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_4_2_0; -.
DR   OMA; MVVYYRL; -.
DR   Proteomes; UP000002506; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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   PANTHER; PTHR30081; PTHR30081; 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; Membrane; Protein transport; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..449
FT                   /note="Protein translocase subunit SecD"
FT                   /id="PRO_0000412674"
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        294..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        317..337
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        379..399
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT   TRANSMEM        401..421
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ   SEQUENCE   449 AA;  48249 MW;  6BB4B5E889798492 CRC64;
     MRRKNGLVFL AILAAMILAF TIVLPTDKGA LLGKGILFGL DLKGGLHMVY QADLSNVDES
     NIDGVMDGVV EVISNRINPL GVTEASIQRQ GDDRIVVELP GLDITDEQKA RIGRTALLEF
     GELAADGEDY KWENSLGKWK PATATIDGVE YTLTSAYFKD STYVNRDQYG NILLVFEWDD
     IGAQLSKEIT TRLLNQQLGI FEGDEALSGD NGIPIAPVIN NVIETSGVIE GLSYNEAEML
     SNQLNAGRLP VPLEPIYEQT VSPTLGQNFV DLAVKAGLVG IILVMIFMIA FYRLPGLLAS
     IALVFYGVIV LALFKLVPVT LTLAGIGGFI VSAGMAVDAN ILIFARLKEE LLTGKTLGAA
     VEAGFSRAWS AIWDSNVTTF IACGILFWVG GTIAAGAPVK GFAVTLFLGV AVSMFTAIFV
     TRTLLRLFVG TKTGKKLALF TTQTRGKNE