SECD_RICBR
ID SECD_RICBR Reviewed; 514 AA.
AC Q1RIN3;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=RBE_0700;
OS Rickettsia bellii (strain RML369-C).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX NCBI_TaxID=336407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RML369-C;
RX PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA Fournier P.-E., Claverie J.-M., Raoult D.;
RT "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT gene exchanges between intracellular pathogens.";
RL PLoS Genet. 2:733-744(2006).
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; CP000087; ABE04781.1; -; Genomic_DNA.
DR RefSeq; WP_011477368.1; NC_007940.1.
DR AlphaFoldDB; Q1RIN3; -.
DR SMR; Q1RIN3; -.
DR STRING; 336407.RBE_0700; -.
DR EnsemblBacteria; ABE04781; ABE04781; RBE_0700.
DR KEGG; rbe:RBE_0700; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_3_5; -.
DR OMA; MVVYYRL; -.
DR OrthoDB; 121331at2; -.
DR Proteomes; UP000001951; 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; IPR001036; Acrflvin-R.
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 PRINTS; PR00702; ACRIFLAVINRP.
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 Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..514
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000272633"
FT TRANSMEM 7..27
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 357..377
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 448..470
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 482..502
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ SEQUENCE 514 AA; 56133 MW; 26DD3694FB47CE20 CRC64;
MQNLPKWKIF LSIICTIFAV ICALPNFTQV KSKYLPHDSV NLGLDLRGGA HLLLDVDFDT
YLNDTMENLA DTLRKSFRED KIGYKNLLVK QNNIQLELRS QEELKPLKRI ISKIDPEINV
EANDNRIKLS YSESRLSELL NKVVDQSIEI VRMRVDSTGT KEPILQKQGD RHILLQVPGE
EDPTYLKNIL GKTAKLIFHL VDENANVEEA VKGHVPMGSM LVQGDRMGYL VVKKKAILGG
DSLTTAAASF DQNSQAVVSF SFNSLGSKLF GEVTKNNVGK HLAIVLDNKL LSAPTINQPI
MGGSGIISGD FTVESANELA LLLRAGSLPA PLKIIEERSI GPNLGADSIE SGKKAGIIGF
AAVCIFMVWS YGLLGLFANI ALSLAMLYVL ALLSLFQATL TLPGIAGIIL TMGMAVDANV
LIYERIKEEL NKGTSNLYAI KTGFESAFAT ILDSNLTTLI VAFLLYIFGV GAIKGFAVAL
TIGIISSMFS AIIITKLLID IWVKYFKPKK LGLV