ID Q89L13_BRADU Unreviewed; 534 AA.
AC Q89L13;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 113.
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:BAC50000.1};
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=224911 {ECO:0000313|EMBL:BAC50000.1, ECO:0000313|Proteomes:UP000002526};
RN [1] {ECO:0000313|Proteomes:UP000002526}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110
RC {ECO:0000313|Proteomes:UP000002526};
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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; BA000040; BAC50000.1; -; Genomic_DNA.
DR RefSeq; NP_771375.1; NC_004463.1.
DR RefSeq; WP_011087503.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89L13; -.
DR STRING; 224911.AAV28_20965; -.
DR EnsemblBacteria; BAC50000; BAC50000; BAC50000.
DR GeneID; 64024491; -.
DR KEGG; bja:bll4735; -.
DR PATRIC; fig|224911.44.peg.4567; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_5; -.
DR InParanoid; Q89L13; -.
DR OrthoDB; 9805019at2; -.
DR PhylomeDB; Q89L13; -.
DR Proteomes; UP000002526; 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:0015031; P:protein transport; IBA:GO_Central.
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; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000002526};
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 375..392
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 468..490
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 496..520
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 162..220
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 355..519
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 534 AA; 57761 MW; B9D8AEDF0AE8F030 CRC64;
MLYFTRWRAL GIILTALIVC LCAVPNFFPE AQVKTWPAWA QRRLVLGLDL QGGSYLLLEV
DSNYVKKERL DQVRDDVRRT LRDAKIGFTG GVTVRNDAAE VRITKETDVQ PALAKLRELA
QPLGGLMGSS GQRDLEVTDA GGGVIRLSIP QAAMLDRMRK TIEQSIQIVE RRVNELGTVE
PVIQRQGNDR ILVQVPGLQD PTRLKELLGK TAKMEFRMVD TSVPPDQAQQ GRLPPESDLL
MSASPPPTPY VVKKQVLVAG GDLTDAQASF DQRTGEPVVS FKFNTSGARK FSQATQENVG
LPFAIVLDNK VISAPVIREP ITGGQGQISG NFTVQSANDL AILLRAGALP APLTVVEERT
VGPGLGQDSI EKGELAAYVG SILVIIFMLV TYRLFGVFAN IAVAINVAMI FGLLSLLNAT
LTLPGIAGIV LTVGIAVDSN VLIYERIREE LRGGRNAISA IDAGFKRALA TILDSNITTF
IAAAVLFYIG TGPVRGFAVT LGIGIITTVF TAFTLTRLIV AGWVRWKRPQ SVPI
//
