ID A0A177H8Q4_9RHOB Unreviewed; 549 AA.
AC A0A177H8Q4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=pfor_17c1919 {ECO:0000313|EMBL:OAH07212.1};
OS Rhodobacteraceae bacterium SB2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=1689867 {ECO:0000313|EMBL:OAH07212.1, ECO:0000313|Proteomes:UP000077333};
RN [1] {ECO:0000313|EMBL:OAH07212.1, ECO:0000313|Proteomes:UP000077333}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB2 {ECO:0000313|EMBL:OAH07212.1,
RC ECO:0000313|Proteomes:UP000077333};
RA Poehlein A., Billerbeck S., Voget S., Wemheuer B., Giebel H.-A.,
RA Brinkhoff T., Daniel R., Simon M.;
RT "A new prominent pelagic Roseobacter clade subcluster - CHAB-I-5:
RT biogeography and genomic comparison to other roseobacters.";
RL Submitted (MAY-2016) 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:OAH07212.1}.
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DR EMBL; LGRT01000018; OAH07212.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A177H8Q4; -.
DR STRING; 1689867.pfor_17c1919; -.
DR PATRIC; fig|1689867.3.peg.1341; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000077333; 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; 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:UP000077333};
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 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 387..405
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 483..505
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 511..535
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 181..238
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 369..539
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 549 AA; 58834 MW; C985795F4CF857ED CRC64;
MLQIDLWKRI VIWGLCIIGL FLALPNAFYT RVEGYNDTKA GLISAESAQD SFAWPSFLPA
SLVNLGLDLR GGAHLLAEVQ VEDVYAARMK ALWPELRDVL RAERAKIGTI RLQKGAADQL
RVKISQAEQI AHAVSAVETL SKPVVSLSNA GARDLEVTSD GDTVIVTLSE AERALTDQRT
LQQALEIIRR RVDEVGTREP TIQRQGARRV LIQVPGIGSA SELKDLIGTT AQLTFQPVIS
RSGNPDVDPG YGNEVLPDLT DADQFYVLEA APVVTGEDLV DAQPSFDQNG RPAVNFRFNP
SGGRRFGDYT ADNIGSPFAI VLDGEVISAP TIQSHISGGS GIITGNFSVE ESTNLAVLLR
AGALPAGLEF LEERTIGPEL GADSIRAGKI ACIVAFAAVL VFMVLSYGLF GLFANVALIV
NVGLIFGLLS LVGATLTLPG IAGIVLTIGM AVDANVLIFE RIREELVSAK GPARAIELGY
EKALSAIIDA NITTFITAVI LFVMGSGPVR GFSITLGLGI LTSVFTAIFV TRLLVVMWFE
RRRPRTLEV
//
