ID A0A059KL20_9BURK Unreviewed; 634 AA.
AC A0A059KL20;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=X805_22150 {ECO:0000313|EMBL:KDB52177.1};
OS Sphaerotilus natans subsp. natans DSM 6575.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Sphaerotilus.
OX NCBI_TaxID=1286631 {ECO:0000313|EMBL:KDB52177.1, ECO:0000313|Proteomes:UP000026714};
RN [1] {ECO:0000313|EMBL:KDB52177.1, ECO:0000313|Proteomes:UP000026714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6575 {ECO:0000313|EMBL:KDB52177.1,
RC ECO:0000313|Proteomes:UP000026714};
RX PubMed=24965827; DOI=10.1111/1574-6941.12372;
RA Park S., Kim D.H., Lee J.H., Hur H.G.;
RT "Sphaerotilus natans encrusted with nanoball-shaped Fe(III) oxide minerals
RT formed by nitrate-reducing mixotrophic Fe(II) oxidation.";
RL FEMS Microbiol. Ecol. 90:68-77(2014).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDB52177.1}.
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DR EMBL; AZRA01000055; KDB52177.1; -; Genomic_DNA.
DR RefSeq; WP_037481803.1; NZ_AZRA01000055.1.
DR AlphaFoldDB; A0A059KL20; -.
DR STRING; 34103.SAMN05421778_102203; -.
DR PATRIC; fig|1286631.3.peg.2179; -.
DR eggNOG; COG0342; Bacteria.
DR Proteomes; UP000026714; Unassembled WGS sequence.
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 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 452..469
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 476..494
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 500..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..595
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 235..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 634 AA; 67830 MW; 678590A39003285B CRC64;
MNRYPWWKYL ILAIAMVVGL LYTLPNFFGE APAVQVSSGK ATLKVDAGLV PRVEQALQAA
GLKPDFVQLE GNSVRARFGD TDTQLKARDA IIRALNPDPA DPSYIVALNL VSRSPQWLTG
LGAQPMYLGL DLRGGVHFLM QVDMAAALTK KTESLAGDVR TLLRDKSIRH AGIQRSGDAI
EVRLRDRETL TKAREALTLA QADMLWTEAG DAAEPRLIGR IKPEAVRNVQ QQALTQNINT
LHNRINELGV AEPVIQQQGA DRVVVQLPGV QDVAKAKDII GRTATLEVRM VDDGPEAQAA
LGGGAPVPFG TERFLERGGV PIIVKRQVVL TGENLTDAQA GFDDNQQPAV HLTLDARGAR
IFRDVTRENI NKRMAILLFE KGKGEVVTAP VIRSEIGGGR VQISGSMTPV EAADTALLLR
AGSLAAPMEI IEERLIGPSL GAENIAKGFD SVLYGFLAIA VFMCAYYMLF GVFSTLALGV
NLLLLVAILS MMQATLTLPG IAAIALVLGM AIDANVLINE RVREELRAGA SPQKAIHMGY
EAAWGTILDS NVTTLIAGVA LLAFGSGPVR GFAVVHCLGI LTSMFSAVLF SRGLVNLWYG
RKKKLQGVSI GQVWKPAAQP GPADAASAVT SPKA
//
