SECD_RHOCB
ID SECD_RHOCB Reviewed; 554 AA.
AC O33517; D5AU88;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 105.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463};
GN OrderedLocusNames=RCAP_rcc01782;
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Rhodobacter.
OX NCBI_TaxID=272942;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=9175857; DOI=10.1006/jmbi.1997.0992;
RA Goldman B.S., Beckman D.L., Bali A., Monika E.M., Gabbert K.K., Kranz R.G.;
RT "Molecular and immunological analysis of an ABC transporter complex
RT required for cytochrome c biogenesis.";
RL J. Mol. Biol. 268:724-738(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX PubMed=20418398; DOI=10.1128/jb.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
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:0000255|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:0000255|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01463}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
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DR EMBL; U69979; AAB62801.1; -; Genomic_DNA.
DR EMBL; CP001312; ADE85527.1; -; Genomic_DNA.
DR RefSeq; WP_013067506.1; NC_014034.1.
DR AlphaFoldDB; O33517; -.
DR SMR; O33517; -.
DR STRING; 272942.RCAP_rcc01782; -.
DR EnsemblBacteria; ADE85527; ADE85527; RCAP_rcc01782.
DR GeneID; 31490657; -.
DR KEGG; rcp:RCAP_rcc01782; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_5; -.
DR OMA; SAHLQMM; -.
DR OrthoDB; 121331at2; -.
DR Proteomes; UP000002361; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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 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 PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR01129; secD; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..554
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000095967"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 392..412
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 414..434
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 491..511
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 516..536
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ SEQUENCE 554 AA; 58943 MW; DF2CBEEBA9F69EDF CRC64;
MLQISLWKRL VILGLCLAAL ITAAPNMFYA RVEGHNDAVS AFEKTGAMTE TQEAAKAAWP
DWAPSALVNL GLDLRGGAHL LAEVHLGEVY KARMDALWPE VRKVLAAERA TIGAIRRVPS
PEGELRIQIG ERAQIARAVE VARTLASPVV SLTGVGQTDY EVTGEGDTVV FRLSEAEKKA
TDDRTMQQSL EIVRRRVDAA GTREPTIMRE GTDRILIEVP GIGSAQELKD LIGTTAKLTF
HPVLSTTSNP NAPVASGNEL LPDAERQGLY HLLDEVPVVT GDDLTDARPT TDDNGAPAVS
FRFNVSGARA FGDYTAGHIG EPFAIVLDGK VISAPTIQAH IAGGSGIITG RFSIEEATDL
ALLLRAGALP AGMTFLEERT IGPELGADSV KAGMVASVIG FVAVVAYMIA SYGLFGFFSS
VALFINIAFI FAVMGAIGGT MTLPGIAGIV LTIGTSVDAN VLIYERMREE IRSGKSPVRA
IELGFDKAMS AIIDANVTSF LSSAILFVLG AGPVRGFAVT TMIGIAASIF TAIWVVRLMI
VIWYGWRRPK TIVI