GenomeNet

Database: UniProt
Entry: Q9RTE3
LinkDB: Q9RTE3
Original site: Q9RTE3 
ID   Q9RTE3_DEIRA            Unreviewed;       768 AA.
AC   Q9RTE3;
DT   01-MAY-2000, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2000, sequence version 1.
DT   07-APR-2021, entry version 131.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01463, ECO:0000256|HAMAP-Rule:MF_01464};
DE   Includes:
DE     RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
DE   Includes:
DE     RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   OrderedLocusNames=DR_1822 {ECO:0000313|EMBL:AAF11371.1};
OS   Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC   Deinococcus.
OX   NCBI_TaxID=243230 {ECO:0000313|EMBL:AAF11371.1, ECO:0000313|Proteomes:UP000002524};
RN   [1] {ECO:0000313|EMBL:AAF11371.1, ECO:0000313|Proteomes:UP000002524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 /
RC   NCIMB 9279 / R1 / VKM B-1422 {ECO:0000313|Proteomes:UP000002524};
RX   PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA   White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA   Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA   Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA   Vamathevan J.J., Lam P., McDonald L., Utterback T., Zalewski C.,
RA   Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA   Ketchum K.A., Nelson K.E., Salzberg S., Smith H.O., Venter J.C.,
RA   Fraser C.M.;
RT   "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT   R1.";
RL   Science 286:1571-1577(1999).
RN   [2] {ECO:0007829|PDB:5XAM, ECO:0007829|PDB:5XAN}
RP   X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 28-768.
RX   PubMed=28467902; DOI=10.1016/j.celrep.2017.04.030;
RA   Furukawa A., Yoshikaie K., Mori T., Mori H., Morimoto Y.V., Sugano Y.,
RA   Iwaki S., Minamino T., Sugita Y., Tanaka Y., Tsukazaki T.;
RT   "Tunnel Formation Inferred from the I-Form Structures of the Proton-Driven
RT   Protein Secretion Motor SecDF.";
RL   Cell Rep. 19:895-901(2017).
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 SecD. 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:0000256|HAMAP-Rule:MF_01464}.
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:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01463}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE000513; AAF11371.1; -; Genomic_DNA.
DR   PIR; F75350; F75350.
DR   RefSeq; NP_295545.1; NC_001263.1.
DR   RefSeq; WP_010888457.1; NZ_CP015081.1.
DR   PDB; 5XAM; X-ray; 4.00 A; A/B=28-768.
DR   PDB; 5XAN; X-ray; 2.75 A; A/B=28-768.
DR   PDB; 5XAP; X-ray; 2.60 A; A=28-768.
DR   PDBsum; 5XAM; -.
DR   PDBsum; 5XAN; -.
DR   PDBsum; 5XAP; -.
DR   SMR; Q9RTE3; -.
DR   STRING; 243230.DR_1822; -.
DR   EnsemblBacteria; AAF11371; AAF11371; DR_1822.
DR   KEGG; dra:DR_1822; -.
DR   PATRIC; fig|243230.17.peg.2034; -.
DR   eggNOG; COG0341; Bacteria.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_3_2_0; -.
DR   InParanoid; Q9RTE3; -.
DR   OMA; RTVNTGM; -.
DR   OrthoDB; 410730at2; -.
DR   Proteomes; UP000002524; Chromosome I.
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:P-P-bond-hydrolysis-driven protein transmembrane transporter 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   HAMAP; MF_01464_B; SecF_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   InterPro; IPR005665; SecF_bac.
DR   InterPro; IPR000731; SSD.
DR   PANTHER; PTHR30081; PTHR30081; 2.
DR   Pfam; PF07549; Sec_GG; 2.
DR   Pfam; PF02355; SecD_SecF; 2.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 2.
DR   TIGRFAMs; TIGR00966; 3a0501s07; 1.
DR   TIGRFAMs; TIGR01129; secD; 1.
DR   PROSITE; PS50156; SSD; 1.
PE   1: Evidence at protein level;
KW   3D-structure {ECO:0007829|PDB:5XAM, ECO:0007829|PDB:5XAN};
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}; Reference proteome {ECO:0000313|Proteomes:UP000002524};
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        33..50
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        295..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        321..341
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        424..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        474..493
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        599..616
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        623..644
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        650..671
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        702..722
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        728..752
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          620..751
FT                   /note="SSD"
FT                   /evidence="ECO:0000259|PROSITE:PS50156"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..18
FT                   /note="Polar"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   768 AA;  82284 MW;  CDFF423F4070B6FD CRC64;
     MTYGSKQVRK TSGSNRRPPP PRRSGGVSRP NPWTALLLLL TLLGSLLYIW RPWEHKNDPW
     SLWNDQYQFM TLGLDLKGGL RIELAPESGT ATRDELDRVK TVIENRINAL GVAEPTVTVS
     GGKRVVVEIP GATPAVQDRA RSIIQQTARL EFRIVNSDAK PDPAVREKNP RSSGYTLAQL
     GPVVATGETI ADATSGTDQR SGQWVVNFKT TDAGAKTFGD FTGKNVNRLM AVVLDDQIQS
     VATINQRLFR DIQISGNFTP EEASQLALVL KSGALPIKIV TAAERSIGPS LGADAIRSGA
     IAALVGIGLV FVMLFAYYGL WFGLVGALGL LFSSIIILGI LGGFGATLTL PGIAGLVLTI
     GAAVDGNVIS FERIKEELAR GKGIKNAIGA GYEHSTAAIL DVNASHLLSA LALYNYSTGA
     VKGFAVTLII GVIASTFSNL VFAKWFMQWL AQRRPNMSAP QWIKHTHFDF MKPAKVITTL
     SVLLALAGAA LVATRGLNYG VDFAPGTTLT ARVDRQVTTE QLRNSVIGAG VSKVTGQSAT
     IQRDTTPGQQ GQNFTVKVPE LNDAEVKQIG AAIGKLPQGQ VLASETVGPA VGKELTQKTI
     YAVLLGLGLI LVYVGFRFDF IMGLGSIIAA IHDVAIAMGL FSLLGLEFTV ASVAALLTLI
     GYSLNDSIIV SDRIRENMKT MRGHSYREIV NAAINQTLSR TVMTSVSTML PLISLLIFGG
     PVLRDFSLIL LVGILVGTYS SIYIVAPLVV YFEEWRDKNR AAKPVTNS
//
DBGET integrated database retrieval system