ID Q3Z9L9_DEHM1 Unreviewed; 449 AA.
AC Q3Z9L9;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463,
GN ECO:0000313|EMBL:AAW40431.1};
GN OrderedLocusNames=DET0333 {ECO:0000313|EMBL:AAW40431.1};
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164 {ECO:0000313|EMBL:AAW40431.1, ECO:0000313|Proteomes:UP000008289};
RN [1] {ECO:0000313|EMBL:AAW40431.1, ECO:0000313|Proteomes:UP000008289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195
RC {ECO:0000313|Proteomes:UP000008289};
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., Deboy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
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 membrane {ECO:0000256|HAMAP-Rule:MF_01463};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01463}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01463}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR EMBL; CP000027; AAW40431.1; -; Genomic_DNA.
DR RefSeq; WP_010936113.1; NC_002936.3.
DR AlphaFoldDB; Q3Z9L9; -.
DR STRING; 243164.DET0333; -.
DR GeneID; 60794308; -.
DR KEGG; det:DET0333; -.
DR PATRIC; fig|243164.10.peg.313; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_2_0; -.
DR InParanoid; Q3Z9L9; -.
DR Proteomes; UP000008289; 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; -; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
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; IPR048631; SecD_1st.
DR InterPro; IPR048634; SecD_SecF_C.
DR NCBIfam; TIGR00916; 2A0604s01; 1.
DR NCBIfam; TIGR01129; secD; 1.
DR PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF21760; SecD_1st; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR00702; ACRIFLAVINRP.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01463};
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};
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 272..292
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 297..317
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 323..345
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 377..396
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 402..425
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 66..122
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 257..427
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 449 AA; 48227 MW; F8B95ACF2231859F CRC64;
MRRKNGLVFL AILAAMILAF TIVLPTDKGA LLGKGILFGL DLKGGLHMVY QADLSNVDES
NIDSVMDGVV EVISNRINPL GVTEASIQRQ GDDRIVVELP GLDITDEQKA RIGRTALLEF
GELAAEGEDY KWENSLGKWK PATATIDGVE YALTSAYFKD STYVNRDQYG NILLVFEWDD
IGAQLSKEIT TRLLSQQLGI FEGDEALAGD DGVPIAPYIN NVIETSGVIE GLSYNEAEML
SNQLNAGRLP VPLEPIYEQT VSPTLGQNFV DLAVKAGLAG IILVMIFMIA FYRLPGLLAS
IALVFYGVIV LALFKLVPVT LTLAGIGGFI VSAGMAVDAN ILIFARLKEE LLAGKTLGAA
VEAGFSRAWS AIWDSNVTTF IACGILFWVG GTIAAGAPVK GFAVTLFLGV AVSMFTAIFV
TRTLLRLFVG TKTAKKLALF TTQTRGKNE
//
