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Database: UniProt
Entry: C4K1K0_RICPU
LinkDB: C4K1K0_RICPU
Original site: C4K1K0_RICPU 
ID   C4K1K0_RICPU            Unreviewed;       518 AA.
AC   C4K1K0;
DT   07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   07-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 69.
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:ACR47451.1};
GN   OrderedLocusNames=RPR_03560 {ECO:0000313|EMBL:ACR47451.1};
OS   Rickettsia peacockii (strain Rustic).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=562019 {ECO:0000313|EMBL:ACR47451.1, ECO:0000313|Proteomes:UP000005015};
RN   [1] {ECO:0000313|EMBL:ACR47451.1, ECO:0000313|Proteomes:UP000005015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Rustic {ECO:0000313|EMBL:ACR47451.1,
RC   ECO:0000313|Proteomes:UP000005015};
RX   PubMed=20027221; DOI=10.1371/journal.pone.0008361;
RA   Felsheim R.F., Kurtti T.J., Munderloh U.G.;
RT   "Genome sequence of the endosymbiont Rickettsia peacockii and comparison
RT   with virulent Rickettsia rickettsii: identification of virulence factors.";
RL   PLoS ONE 4:E8361-E8361(2009).
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 inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {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; CP001227; ACR47451.1; -; Genomic_DNA.
DR   AlphaFoldDB; C4K1K0; -.
DR   KEGG; rpk:RPR_03560; -.
DR   HOGENOM; CLU_007894_4_3_5; -.
DR   Proteomes; UP000005015; 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; -; 2.
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 inner membrane {ECO:0000256|ARBA:ARBA00022519, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
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        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        361..394
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        448..473
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        479..503
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          144..203
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          337..504
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   518 AA;  56674 MW;  2DF50D0F0286DA17 CRC64;
     MQNLPKWKIF LSIICTVFAV ICALPNFMQV NSKFLPHDSV NLGLDLRGGA HLLLDVDFDT
     YLNDSMENLA DTLRKNFRED KIGYKNLLVR QNSIQLEVRS PEKLKPLKKI INKIDPEIIA
     EVNENKIKLS YSESRLNDLL NKVVDQSIEI VRMRVDSTGT KEPTLQKQGD KHILLQVPGE
     ENPSYLKNIL GKTAKLTFHL VDENANIEEA VKGHVPVGSM LVKGDNESHG EYYVVIKKKV
     VLGGDQLTTA SASFDQNSQA VVAFSFNNLG SKIFGEITKN NTGKRLAIVL DNKLLSAPTI
     NGAIMGGRGI ITGNFTVESA NELALLLQAG SLPAPLKIIE ERSIGPNLGA DSIESGKKAE
     LIGFIAVCIF MVWSYGVLGL FANIALSLAL LYILALLSLF QATLTLPGIA GIILTMGMAV
     DANVLIYERI KEELHKGVSN LYAIRTGFES AFATILDANL TTLIVAFLLY IFGVGAIKGF
     AVALTIGIIS SMFSAIIITK LLIDIWVQYF KPKKLGLV
//
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