ID A0A0D6B5V7_RHOSU Unreviewed; 553 AA.
AC A0A0D6B5V7;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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:BAQ70099.1};
GN ORFNames=NHU_02952 {ECO:0000313|EMBL:BAQ70099.1};
OS Rhodovulum sulfidophilum (Rhodobacter sulfidophilus).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=35806 {ECO:0000313|EMBL:BAQ70099.1, ECO:0000313|Proteomes:UP000064912};
RN [1] {ECO:0000313|EMBL:BAQ70099.1, ECO:0000313|Proteomes:UP000064912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2351 {ECO:0000313|EMBL:BAQ70099.1,
RC ECO:0000313|Proteomes:UP000064912};
RA Nagao N.;
RT "Genome sequene of Rhodovulum sulfidophilum DSM 2351.";
RL Submitted (FEB-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}.
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DR EMBL; AP014800; BAQ70099.1; -; Genomic_DNA.
DR RefSeq; WP_060835452.1; NZ_AP014800.1.
DR AlphaFoldDB; A0A0D6B5V7; -.
DR KEGG; rsu:NHU_02952; -.
DR PATRIC; fig|35806.4.peg.3035; -.
DR eggNOG; COG0342; Bacteria.
DR Proteomes; UP000064912; Chromosome.
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; IPR001036; Acrflvin-R.
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 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};
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 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 186..242
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 373..543
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 553 AA; 59369 MW; 6DB9EAC057CC3363 CRC64;
MLDFALWKRV AIWGVVLLGL LFAAPNMFYS RVEGHNDALK AIETQGATPE LIAKRDGWPG
WLPSGLVNLG LDLRGGAHLL AEVQVEDVYA DRMDALWPDV RDALREVRDR VGPIRRIDGT
PGTLQVRLGE PAGMPAALEA VRGLARPIVS LTGIGASDID VSGEGAVLTV QLSEPEKQAT
IDRTLRQSLE IVRRRIDEVG TREPTIQRQG EDRILIEVPG IGSADELKAL IGTTARLTFN
PVVSRTSNPN EAPGASNELL PSMDEPGTYY IIEKTPVVSG EELTDSQPAF DQNGEPSVTF
RFNPSGARKF GQYTAEHVGS PFAIVLDDEV ISAPVIREAI PSGSGQITGN FTVEESTQLA
VLLRAGALPA ELTFLEERTI GPQLGADSIE AGKIASAAAF LLVLLFMWAS YGLFGLFANV
ALIVNIGLIF GLLSMIGATL TLPGIAGIVL TIGMAVDANV LVFERIREEL KTAKGPARAI
ELGYQRALSA ILDANITTFL TAVILFVMGS GPVRGFAVTL AIGIVTSVFV AIYVTRMMIV
MWMARRRPKS IVL
//
