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Database: UniProt
Entry: A0A553WHE5_9SPHN
LinkDB: A0A553WHE5_9SPHN
Original site: A0A553WHE5_9SPHN 
ID   A0A553WHE5_9SPHN        Unreviewed;       532 AA.
AC   A0A553WHE5;
DT   16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2019, sequence version 1.
DT   24-JAN-2024, entry version 13.
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:TSB04123.1};
GN   ORFNames=FOM92_01410 {ECO:0000313|EMBL:TSB04123.1};
OS   Sphingorhabdus contaminans.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingorhabdus.
OX   NCBI_TaxID=1343899 {ECO:0000313|EMBL:TSB04123.1, ECO:0000313|Proteomes:UP000320160};
RN   [1] {ECO:0000313|EMBL:TSB04123.1, ECO:0000313|Proteomes:UP000320160}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC32445 {ECO:0000313|EMBL:TSB04123.1,
RC   ECO:0000313|Proteomes:UP000320160};
RA   Park M.;
RL   Submitted (JUL-2019) 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}.
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:TSB04123.1}.
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DR   EMBL; VKKU01000001; TSB04123.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A553WHE5; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000320160; 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; -; 1.
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; 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   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        371..389
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        396..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        421..441
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        469..488
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        494..518
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          158..217
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          350..514
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   532 AA;  56915 MW;  2A079AD194808EC3 CRC64;
     MLDFPRWRVW MLSLLVLVGV LLAIPSVLPT SIRAQLAQFV PTPTINLGLD LAGGSHILLE
     ADTSQLAETR LEALEDSVRS AMRRTDPRIA IGNVSRANGQ LSFTVTDSSQ VDAAREALLP
     LTSNTLGSRD WNIGVNDGNR IVLSPASTGN ETALDQAMDT AKDVIDRRIN ALGTLEPTII
     RQGENRIVVQ VPGLEDPEAL KALIGKTAKL EFKLVDEQAD PDQTAKGIAR VGSQVLPYPD
     NPSGLPNIAV RRLGGISGDK LIKADPTFDQ QTNEPAVTIQ FDSEGGQKFA RMTQQNTGKL
     FAIILDGQVI SAPQIKEPIF GGISQISGSF TVESANALSI SLRSGALPVD LKIVEERSVG
     PDLGADSIRR GILAAVIGTT SILVLMFAVY GRFGMYANIA LVINIGLILG VMALANATLT
     LPGIAGFVLT IGAAVDANVL INERIREELK RGRRVVQAIE FGYKEASRAI FDANSTNVIA
     AVLLFIFGSG PIRGFAVVLM IGIVTSVFTA VTLTRMWVAG WVKRTRPQEL VI
//
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