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Database: UniProt
Entry: A0A0H0XKK5_9SPHN
LinkDB: A0A0H0XKK5_9SPHN
Original site: A0A0H0XKK5_9SPHN 
ID   A0A0H0XKK5_9SPHN        Unreviewed;       532 AA.
AC   A0A0H0XKK5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=AAV99_10705 {ECO:0000313|EMBL:KLI63153.1};
OS   Aurantiacibacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Erythrobacteraceae; Aurantiacibacter.
OX   NCBI_TaxID=874156 {ECO:0000313|EMBL:KLI63153.1, ECO:0000313|Proteomes:UP000053455};
RN   [1] {ECO:0000313|EMBL:KLI63153.1, ECO:0000313|Proteomes:UP000053455}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HWDM-33 {ECO:0000313|EMBL:KLI63153.1,
RC   ECO:0000313|Proteomes:UP000053455};
RA   Zhuang L., Liu Y., Shao Z.;
RT   "The draft genome sequence of Erythrobacter marinus HWDM-33.";
RL   Submitted (APR-2015) 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:KLI63153.1}.
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DR   EMBL; LBHU01000003; KLI63153.1; -; Genomic_DNA.
DR   RefSeq; WP_047094048.1; NZ_LDCP01000003.1.
DR   AlphaFoldDB; A0A0H0XKK5; -.
DR   STRING; 874156.GCA_001021555_02296; -.
DR   PATRIC; fig|874156.12.peg.2196; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000053455; 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000053455};
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        368..388
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        395..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          157..215
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          350..518
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   532 AA;  56802 MW;  17DD88C49135F401 CRC64;
     MLDFPLWKRI TLWVITLGFA FAALPSIAGL AGLDLPDSLE GPEINLGLDL AGGSHILLEA
     DPSQVAEQRL ESAEESVRDL LANAEPRIAI GDLSTLDNQL SFMLENPSDI DRAREELRDL
     INGTGLVAEW RLDVVDGNRM VLTQTEQGLD EAVEGAMESA TEVVRRRIDA LGTREPTIIR
     QGDSRIVVQV PGLEDPDALK ALLGETAELE FKLVDANALP SDVAQGIANP GSEIVPYAED
     SDFAGQFEAV RRLGGIRGDR LTGAQQGVNP QTNETVVNIQ FDPQGGARFA QLSTENVGRR
     FAIILDDHVI SAPNFNEPIL GGAAQISGGF TTETANNLAI QLRSGALPVD LTVIEERTVG
     PDLGRDSIVK GGIAMAVGSL LVIALMIASY GRFGVYATGA LVLNVLMILG IMALINSTLT
     LPGIAGFVLT IGAAVDANVL INERIREERK RGRRVVAAVE NGYKEASRAI YDANITNFIA
     GALLLGFGSG PVRGFAVVLI IGLITTVFTA VFITRMWVAG WLRAKRPTEI TV
//
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