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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
 
 
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