ID Q5WV40_LEGPL Unreviewed; 618 AA.
AC Q5WV40;
DT 23-NOV-2004, integrated into UniProtKB/TrEMBL.
DT 23-NOV-2004, sequence version 1.
DT 27-MAR-2024, entry version 104.
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:CAH16217.1};
GN OrderedLocusNames=lpl1977 {ECO:0000313|EMBL:CAH16217.1};
OS Legionella pneumophila (strain Lens).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=297245 {ECO:0000313|EMBL:CAH16217.1, ECO:0000313|Proteomes:UP000002517};
RN [1] {ECO:0000313|EMBL:CAH16217.1, ECO:0000313|Proteomes:UP000002517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Lens {ECO:0000313|EMBL:CAH16217.1,
RC ECO:0000313|Proteomes:UP000002517};
RX PubMed=15467720; DOI=10.1038/ng1447;
RA Cazalet C., Rusniok C., Bruggemann H., Zidane N., Magnier A., Ma L.,
RA Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F., Etienne J.,
RA Glaser P., Buchrieser C.;
RT "Evidence in the Legionella pneumophila genome for exploitation of host
RT cell functions and high genome plasticity.";
RL Nat. Genet. 36:1165-1173(2004).
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-YajC and YidC. {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 -!- 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; CR628337; CAH16217.1; -; Genomic_DNA.
DR RefSeq; WP_011215965.1; NC_006369.1.
DR AlphaFoldDB; Q5WV40; -.
DR KEGG; lpf:lpl1977; -.
DR LegioList; lpl1977; -.
DR HOGENOM; CLU_007894_4_3_6; -.
DR Proteomes; UP000002517; 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; IPR001036; Acrflvin-R.
DR InterPro; IPR005791; SecD.
DR InterPro; IPR027398; SecD-TM.
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:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF13721; SecD-TM1; 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 inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
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 455..474
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 550..572
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 578..606
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 3..102
FT /note="SecD export protein N-terminal TM"
FT /evidence="ECO:0000259|Pfam:PF13721"
FT DOMAIN 227..286
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 439..605
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 618 AA; 67303 MW; 77D05F967E12F539 CRC64;
MQNKYPLWKN LMLIVIAVIG FVYAIPNLYT ENPVVQISAG TDEDTETIKN QVESILKNAN
MDYKSLVVER DGVEVVFSST DSQLLARDVI KNSLGSDYTV ALNLAPSTPA WLEAIHADPM
KQGLDLRGGV HFLLEVDVES VISRRYEGIM KNIGQELREA GIRYSGIRYL SDKGIELRFR
DSDSMENALV ELRQKISDVV FVKTKTQNSI LGAISPAELN SIRQNTIEQT MSILRNRVNE
LGVGEAVVQQ QGATRVAVDL PGIQDAARAK QILGGTATLE FHLVDQENDP FIAKQTGVVP
VNDKLYMMDG HPILLKRQVV LSGDSITSAV SSFDQQTASP SVQIQLGGGG ESLFTKVTRE
NIGKRMAIVF VETKTTTQTI NGEEKRVTKK EERVISAPVI QNALGSNFQI TGLTDSKEAS
NLALLLRAGA LPAAIYPVEE RTVGPTLGKE NIRRGLISLE VGMGLILALM LVYYHFFGLI
ADIALMLNLV FLCALLSIID ATLTLPGIAG IVLTVGMAVD ANVLIYERIR EELRNGLSPQ
AAIHAGYERA FSTILDANVT TLIVAIILFA VGTGPVRGFA VVLSLGLLTS MLTGITYTRA
IVNWYYGGRN VKKLSIGI
//
