SECD_STRCO
ID SECD_STRCO Reviewed; 570 AA.
AC Q53955; Q9L293;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 25-MAY-2022, entry version 130.
DE RecName: Full=Protein translocase subunit SecD {ECO:0000255|HAMAP-Rule:MF_01463};
GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=SCO1516;
GN ORFNames=SCL2.06c;
OS Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces; Streptomyces albidoflavus group.
OX NCBI_TaxID=100226;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=A3(2) / NRRL B-16638;
RA Loriaux A., Frare P., Brans A., Dusart J.;
RL Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-471 / A3(2) / M145;
RX PubMed=12000953; DOI=10.1038/417141a;
RA Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT A3(2).";
RL Nature 417:141-147(2002).
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. Other proteins may also be involved.
CC {ECO:0000255|HAMAP-Rule:MF_01463}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01463};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-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; X85969; CAA59954.1; -; Genomic_DNA.
DR EMBL; AL939109; CAB70918.1; -; Genomic_DNA.
DR PIR; S52765; S52765.
DR RefSeq; NP_625795.1; NC_003888.3.
DR RefSeq; WP_011027823.1; NC_003888.3.
DR AlphaFoldDB; Q53955; -.
DR SMR; Q53955; -.
DR STRING; 100226.SCO1516; -.
DR GeneID; 1096942; -.
DR KEGG; sco:SCO1516; -.
DR PATRIC; fig|100226.15.peg.1525; -.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_4_2_11; -.
DR InParanoid; Q53955; -.
DR OMA; WPRARRT; -.
DR PhylomeDB; Q53955; -.
DR Proteomes; UP000001973; 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:0015031; P:protein transport; IBA:GO_Central.
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 InterPro; IPR022646; SecD/SecF_CS.
DR PANTHER; PTHR30081; PTHR30081; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR TIGRFAMs; TIGR01129; secD; 1.
PE 3: Inferred from homology;
KW Cell membrane; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..570
FT /note="Protein translocase subunit SecD"
FT /id="PRO_0000095971"
FT TRANSMEM 370..390
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 419..439
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 474..494
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT TRANSMEM 498..518
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01463"
FT REGION 104..198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 540..570
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 104..121
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 147..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..198
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 72
FT /note="Y -> N (in Ref. 1; CAA59954)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="S -> K (in Ref. 1; CAA59954)"
FT /evidence="ECO:0000305"
FT CONFLICT 550..551
FT /note="PL -> SV (in Ref. 1; CAA59954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 570 AA; 59511 MW; 073ADE27F2B921E3 CRC64;
MFASGHTTPR LGIDLAGGTS ITLRAVPEAG QESAINKTNM DTAVEIMNRR VNGLGVSEAE
VQTQGDRNII VYIPKGTNSK EARQQVGTTA KLYFRPVLAT ELSGANATGT PSASETGGAS
DKATDKATDK ATDKATDGDK ATDGDKASGT PSDSASASAT SQGRAASDAL KADPSPSATS
SDGASPSPSA SASGDDATAK LQQQYAALDC TDKNARAKAG DGAKPDEQTV ACGQNSQGQW
QKYILGAAAV DGTEVDEAEA VYNTQTAAGW TVTMKFTDKG SKKFADITGK LAQNQSPQNQ
FAIVLDNEVV SDPYVSQALT GGNAEISGSF DQEEAQSLAN MLSYGALPLT FKEDSVTTVT
AALGGEQLKA GLIAGAIGLA LVVLYLLFYY RGLSFIAVCS LLVSAGLTYV IMALLGPTIG
FALNLPAVCG AIVAIGITAD SFIVYFERVR DEIREGRTLR PAVERAWPRA RRTILVSDFV
SFLAAAVLFI VTVGKVQGFA FTLGLTTLLD VVVVFLFTKP LLTLMARRKF FASGHKWSGL
DPKALGAKPP LRRTRRPSRP AAGPVDPKEA
