ID T0HVD1_9SPHN Unreviewed; 532 AA.
AC T0HVD1;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=L485_10350 {ECO:0000313|EMBL:EQB01469.1};
OS Sphingobium baderi LL03.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1114964 {ECO:0000313|EMBL:EQB01469.1, ECO:0000313|Proteomes:UP000015524};
RN [1] {ECO:0000313|EMBL:EQB01469.1, ECO:0000313|Proteomes:UP000015524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL03 {ECO:0000313|EMBL:EQB01469.1,
RC ECO:0000313|Proteomes:UP000015524};
RX PubMed=24051322;
RA Kaur J., Verma H., Tripathi C., Khurana J.P., Lal R.;
RT "Draft Genome Sequence of a Hexachlorocyclohexane-Degrading Bacterium,
RT Sphingobium baderi Strain LL03T.";
RL Genome Announc. 1:e00751-13(2013).
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:EQB01469.1}.
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DR EMBL; ATIB01000059; EQB01469.1; -; Genomic_DNA.
DR RefSeq; WP_021244933.1; NZ_KQ130472.1.
DR AlphaFoldDB; T0HVD1; -.
DR PATRIC; fig|1114964.3.peg.2023; -.
DR eggNOG; COG0342; Bacteria.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000015524; 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 HAMAP; MF_01463_B; SecD_B; 1.
DR InterPro; IPR001036; Acrflvin-R.
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 PRINTS; PR00702; ACRIFLAVINRP.
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:UP000015524};
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 470..489
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 495..522
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 159..217
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 352..522
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 532 AA; 57017 MW; 6043F78651B04C14 CRC64;
MLNFSRWAVA AILLPLVIGI LCAVPSFLPE QAVEKLPRFM QTRVNLGLDL SGGSHLLLEA
STQDVAKQRL TNMEEQVRTE LRRGDPRIAV GDISSRDGKL SFMVRDPAQV DAAVERIRPL
TQGAGLTGQR DFNVEVVNSS TIVITPTDAG INNAVKSAME VATEVIRKRI DEMGTREPTI
QQQGDNRIVV QVPGLQNPKA LKDLLGQTAK LEFKLVDVTA NPAEVAQGRA PVGSEVLPYP
DNPSRVPVIA VKRQVMVSGE DLTDATQGYD QNNQAIVNIR FNGSGGRKFG QVTSQNVNRP
FAIILDGRVL SAPNINEPIL GGSAQISGNF TVESANQLAI ALRSGKLPVA LTVVEERTVG
PQLGADSIRA GLIASVIAVV AVAAFMFFSY GRFGVYANIA VTINVLVILG VMGILGATLT
LPGIAGFVLT IGTAVDANVL IYERIREERR RGRGVVQAIE YGYKEASRTI FEANVTHAIA
GGIMLALGSG PIKGFAIVLL IGIATSVYTA VTFTRVLAAW WLRTKRPTEI NI
//