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Database: UniProt
Entry: A0A126ZCR0_9BURK
LinkDB: A0A126ZCR0_9BURK
Original site: A0A126ZCR0_9BURK 
ID   A0A126ZCR0_9BURK        Unreviewed;       629 AA.
AC   A0A126ZCR0;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=AX767_11330 {ECO:0000313|EMBL:AMM24883.1};
OS   Variovorax sp. PAMC 28711.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM24883.1, ECO:0000313|Proteomes:UP000070169};
RN   [1] {ECO:0000313|EMBL:AMM24883.1, ECO:0000313|Proteomes:UP000070169}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM24883.1,
RC   ECO:0000313|Proteomes:UP000070169};
RA   Park H.;
RT   "Complete genome of Variovorax sp.";
RL   Submitted (FEB-2016) 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 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; CP014517; AMM24883.1; -; Genomic_DNA.
DR   RefSeq; WP_068631396.1; NZ_CP014517.1.
DR   AlphaFoldDB; A0A126ZCR0; -.
DR   STRING; 1795631.AX767_11330; -.
DR   KEGG; vaa:AX767_11330; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000070169; 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; IPR005791; SecD.
DR   InterPro; IPR027398; SecD-TM.
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; 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 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:UP000070169};
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        452..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        547..567
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        573..599
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          1..108
FT                   /note="SecD export protein N-terminal TM"
FT                   /evidence="ECO:0000259|Pfam:PF13721"
FT   DOMAIN          234..293
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"
SQ   SEQUENCE   629 AA;  67624 MW;  DAD13BB4B27E2530 CRC64;
     MNRYPVWKYA VIVIVLLVGL IYALPNFFGE APAVQVSAAK STVKVDAATQ ARVDEALKAA
     GLVPDMQTID ATSLRVRFTT TDDQLKARDV MQRALVPDPA DPPYTVALNL VPRSPAWLAA
     LHAYPMYLGL DLRGGVDFML QVDMKGAIDK KAETFSSDLR SALRDKSIRG SAVNRNGQAI
     EVSFRDAASL EAARVLVTDQ FPDLTPTTAQ NGGDFKLTAT IKPEAARRLQ DAALKQNITT
     LHNRINELGV AEPVIQQQGL DRIVVQLPGV QDTAKAKDIL GRTATLEMRM VDETAEGRAA
     ETGSGPVPFG SEKFLDRTGR AVIVKKQVLV TGENLTDAQP GFDSQSNQPK VDLTMDAKGG
     RIMRDVSRDN YKKRMAMLIF EKGKGEVLTA PSINGELGNR FQISGSMNVV EANDLALLLR
     AGSLAAPMEI IQERTIGPSL GADNIKKGFD SVMYGFVAIM VFMCLYYALF GAFSSIALAV
     NLMLLVAILS MLQATLTLPG IAAMALAIGV AIDSNVLINE RVREELRNGA SPQAAIHAGY
     DRAWGTILDA NVTTLIAGVA LLAFGSGPIR GFAVVHCIGI VTSMFSAVFF SRGLVNLWYG
     RKKKLKSVSI GTVWRPKTDA AGTALAEAK
//
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