ID X6L4Y9_9RHOB Unreviewed; 553 AA.
AC X6L4Y9;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-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=P279_07245 {ECO:0000313|EMBL:ETA52684.1};
OS Rhodobacteraceae bacterium PD-2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA52684.1, ECO:0000313|Proteomes:UP000023196};
RN [1] {ECO:0000313|EMBL:ETA52684.1, ECO:0000313|Proteomes:UP000023196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PD-2 {ECO:0000313|EMBL:ETA52684.1,
RC ECO:0000313|Proteomes:UP000023196};
RX PubMed=25700405;
RA Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT Prorocentrum donghaiense.";
RL Genome Announc. Announc.3:e01549-14(2015).
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:ETA52684.1}.
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DR EMBL; AWRV02000007; ETA52684.1; -; Genomic_DNA.
DR AlphaFoldDB; X6L4Y9; -.
DR PATRIC; fig|1169855.3.peg.1306; -.
DR HOGENOM; CLU_007894_4_3_5; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000023196; 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; 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; 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:UP000023196};
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 445..466
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 487..509
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 515..539
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 185..242
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 376..543
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 553 AA; 59311 MW; A524D97D165D5631 CRC64;
MLQIDSWKRV LIWSTLVVGI AFAAPNLFYG RVEGHNDAVK AIEAGADTSE NREAASAWPS
WLPSGLVNLG LDLRGGAHLL AEVQVSDVYA ARMESLWPEV RDVLRDERAT VGTIRLQDGP
PDELRVRISE PGGMERAIEL VRGLSTPVVS LTGQGTRDIE VFGDGSDLVV TLSEAERQAI
DERTLQQTLE IVRRRIDEVG TREPTIQRQG GDRVLIQVPG LGSAQELKDL IGTTAQLTFQ
PVISRTGSAN DNPGVGNEVV PSLDEEGVFY ILEQAPVVTG EELVDARPDF DQNGRPAVSF
RFNPSGGRKF GDYTAANIGS PFAIVLDNEV ISAPVIQSHI SGGSGIITGN FTVEESTNLA
VLLRAGALPA GLDFLEERTI GPELGQDSID AGKIATMVAF AAVLVFMVLS YGLFGVFANI
ALILNIGLMF GFLSSFGATL TLPGIAGIVL TVGMAVDANV LVFERIREEL KTARGPARAI
ELGYEKALSA IVDANITTFI TAVILYVMGA GPVRGFAVTL GVGILTSVFT AIFVTRLLIV
MWFERRRPKT IEV
//
