SECD_RICCN
ID SECD_RICCN Reviewed; 518 AA.
AC Q92H77;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=RC0894;
OS Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX NCBI_TaxID=272944;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-613 / Malish 7;
RX PubMed=11557893; DOI=10.1126/science.1061471;
RA Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL Science 293:2093-2098(2001).
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; AE006914; AAL03432.1; -; Genomic_DNA.
DR PIR; F97811; F97811.
DR RefSeq; WP_010977497.1; NC_003103.1.
DR AlphaFoldDB; Q92H77; -.
DR SMR; Q92H77; -.
DR EnsemblBacteria; AAL03432; AAL03432; RC0894.
DR KEGG; rco:RC0894; -.
DR PATRIC; fig|272944.4.peg.1018; -.
DR HOGENOM; CLU_007894_4_3_5; -.
DR OMA; MVVYYRL; -.
DR Proteomes; UP000000816; 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..518
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000272634"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 384..404
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 406..426
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 452..474
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 486..506
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
SQ SEQUENCE 518 AA; 56516 MW; 4487A46517B65CE4 CRC64;
MQKLPKWKIF LSIICTVFAV ICALPNFMQV NSKFLPHDSV NLGLDLRGGA HLLLDVDFDT
YLNDSMENLA DTLRKNFRED KIGYKNLLVR QNSIQLEVRS PEKLKPLKKI INKIDPEIIA
EVNENKIKLS YSESRLNDLL NKVVDQSIEI VRMRVDSTGT KEPTLQKQGD KHILLQVPGE
ENPSYLKNIL GKTAKLTFHL VDENANIEEA VKGHVPVGSM LVKGDNASHG EYYVVIKKKV
VLGGDQLTTA SASFDQNSQA VVAFSFNNLG SKIFGEITKN NIGKRLAIVL DNKLLSAPTI
NGAIMGGSGI ITGNFTVESA NELALLLRAG SLPAPLKIIE ERSIGPNLGA DSIESGKKAG
LIGFIAVCIF MVWSYGVLGL FANIALSLAL LYILALLSLF QATLTLPGIA GIILTMGMAV
DANVLIYERI KEELHKGVST LYAIRTGFES AFATILDANL TTLIVAFLLY IFGVGAIKGF
AVALTIGIIS SMFSAIIITK LLIDIWVQYF KPKKLGLV