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
//