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Database: UniProt
Entry: A4JBP0_BURVG
LinkDB: A4JBP0_BURVG
Original site: A4JBP0_BURVG 
ID   A4JBP0_BURVG            Unreviewed;       673 AA.
AC   A4JBP0;
DT   01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   OrderedLocusNames=Bcep1808_0681 {ECO:0000313|EMBL:ABO53693.1};
OS   Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS   (strain R1808)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=269482 {ECO:0000313|EMBL:ABO53693.1, ECO:0000313|Proteomes:UP000002287};
RN   [1] {ECO:0000313|Proteomes:UP000002287}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G4 / LMG 22486 {ECO:0000313|Proteomes:UP000002287};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000614; ABO53693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4JBP0; -.
DR   KEGG; bvi:Bcep1808_0681; -.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_4_3_4; -.
DR   Proteomes; UP000002287; Chromosome 1.
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; 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   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:UP000002287};
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        6..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        452..476
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        496..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        539..565
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        571..599
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          1..112
FT                   /note="SecD export protein N-terminal TM"
FT                   /evidence="ECO:0000259|Pfam:PF13721"
FT   DOMAIN          238..296
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          428..598
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   REGION          636..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   673 AA;  71492 MW;  9E90FEE87AABD47B CRC64;
     MNRYPIWKYV VMVVALAIGF LYTLPNFFGE APAVQVSSGK ATVKLDSATL SQVEAALASA
     QIKPDDVTFE NTATNANIRV RLKDTDTQLR VKDLLQKSLN TDPNDPQYVV ALNLQSASPR
     WLTAIHALPM YLGLDLRGGV HFLLQVDMTG ALTKKLDSDA TDARALLRDK NIRDGGVSRV
     DQSVVVNFSD AQTAEDALKA LAASITELQW ATQPGGGGTQ VVGTFTPAVQ KSVEDAALKQ
     NLTTLHNRVN ELGVSEPILQ QQGSDRIVVE LPGVQDTAKA KDIIGRTATL EARLADPINT
     HPNPNDPVPP GEELFTQGNQ APVLLKKDVI FTGDRIIDAS AGFDEHQRPS VNIRLDSAGG
     RSVRAVSREN IGKPMAMVLF EKGKGEVLTV ATIQSELGDR FQITGQPTPQ AAADLALLLR
     AGSLAAPMDI IEERTIGPSL GADNIKMGVH SVIWGFCAIA VFMVAYYMLF GVISVIGLSV
     NLLLLVAVLS LMQATLTLPG IAAIALALGM AIDSNVLINE RVREELRAGQ PPQLAIQSGY
     AHAWATILDS NVTTLIAGLA LLAFGSGPVR AFAIVHCLGI LTSMFSAVFF SRGIVNLWYG
     GRKKLKSLAI GQVWKPEGAA AGATFAAADE STDTARAAKL AAPAKGNGPR AGKPQLRNRA
     QPGVPPKKPG STQ
//
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