SECDF_THET8
ID SECDF_THET8 Reviewed; 735 AA.
AC Q5SKE6;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Protein translocase subunit SecDF;
GN Name=secDF; OrderedLocusNames=TTHA0697;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), SUBUNIT, UTILIZATION OF PMF, AND
RP MUTAGENESIS OF ASP-340; ASP-637 AND ARG-671.
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RX PubMed=21562494; DOI=10.1038/nature09980;
RA Tsukazaki T., Mori H., Echizen Y., Ishitani R., Fukai S., Tanaka T.,
RA Perederina A., Vassylyev D.G., Kohno T., Maturana A.D., Ito K., Nureki O.;
RT "Structure and function of a membrane component SecDF that enhances protein
RT export.";
RL Nature 474:235-238(2011).
CC -!- FUNCTION: Conducts protons, which can be regulated by a proton gradient
CC or by binding of an unfolded protein. Proton conduction requires the
CC large periplasmic domain of the SecD.
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.
CC -!- SUBUNIT: Part of the essential Sec protein translocation apparatus
CC which comprises SecA, SecYEG and auxiliary protein SecDF. Other
CC proteins may also be involved (By similarity). Monomer. {ECO:0000250,
CC ECO:0000269|PubMed:21562494}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the SecD/SecF family.
CC SecD subfamily. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the SecD/SecF family.
CC SecF subfamily. {ECO:0000305}.
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DR EMBL; AP008226; BAD70520.1; -; Genomic_DNA.
DR RefSeq; WP_011172795.1; NC_006461.1.
DR RefSeq; YP_143963.1; NC_006461.1.
DR PDB; 2RRN; NMR; -; A=470-559.
DR PDB; 3AQO; X-ray; 2.60 A; A/B/C/D=35-263.
DR PDB; 3AQP; X-ray; 3.30 A; A/B=1-735.
DR PDB; 5YHF; X-ray; 2.80 A; A=1-735.
DR PDBsum; 2RRN; -.
DR PDBsum; 3AQO; -.
DR PDBsum; 3AQP; -.
DR PDBsum; 5YHF; -.
DR AlphaFoldDB; Q5SKE6; -.
DR BMRB; Q5SKE6; -.
DR SMR; Q5SKE6; -.
DR STRING; 300852.55772079; -.
DR TCDB; 2.A.6.4.3; the resistance-nodulation-cell division (rnd) superfamily.
DR EnsemblBacteria; BAD70520; BAD70520; BAD70520.
DR GeneID; 3168575; -.
DR KEGG; ttj:TTHA0697; -.
DR PATRIC; fig|300852.9.peg.691; -.
DR eggNOG; COG0341; Bacteria.
DR eggNOG; COG0342; Bacteria.
DR HOGENOM; CLU_007894_3_2_0; -.
DR OMA; RTVNTGM; -.
DR PhylomeDB; Q5SKE6; -.
DR Proteomes; UP000000532; 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 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.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..735
FT /note="Protein translocase subunit SecDF"
FT /id="PRO_0000412713"
FT TRANSMEM 1..24
FT /note="Helical; Name=1"
FT /evidence="ECO:0000305"
FT TOPO_DOM 25..268
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 269..293
FT /note="Helical; Name=2"
FT /evidence="ECO:0000305"
FT TRANSMEM 294..315
FT /note="Helical; Name=3"
FT /evidence="ECO:0000305"
FT TOPO_DOM 316..324
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 325..347
FT /note="Helical; Name=4"
FT /evidence="ECO:0000305"
FT TOPO_DOM 348..360
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 361..390
FT /note="Helical; Name=5"
FT /evidence="ECO:0000305"
FT TOPO_DOM 391..396
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 397..425
FT /note="Helical; Name=6"
FT /evidence="ECO:0000305"
FT TOPO_DOM 426..444
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 445..468
FT /note="Helical; Name=7"
FT /evidence="ECO:0000305"
FT TOPO_DOM 469..565
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 566..589
FT /note="Helical; Name=8"
FT /evidence="ECO:0000305"
FT TRANSMEM 590..615
FT /note="Helical; Name=9"
FT /evidence="ECO:0000305"
FT TOPO_DOM 616..620
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 621..646
FT /note="Helical; Name=10"
FT /evidence="ECO:0000305"
FT TOPO_DOM 647..660
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 661..688
FT /note="Helical; Name=11"
FT /evidence="ECO:0000305"
FT TOPO_DOM 689..692
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 693..723
FT /note="Helical; Name=12"
FT /evidence="ECO:0000305"
FT TOPO_DOM 724..735
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..434
FT /note="SecD"
FT REGION 112..248
FT /note="Required for proton transport"
FT REGION 435..735
FT /note="SecF"
FT MUTAGEN 340
FT /note="D->N: Abolishes ion channel activity."
FT /evidence="ECO:0000269|PubMed:21562494"
FT MUTAGEN 637
FT /note="D->N: No effect on ion channel activity."
FT /evidence="ECO:0000269|PubMed:21562494"
FT MUTAGEN 671
FT /note="R->M: Abolishes ion channel activity."
FT /evidence="ECO:0000269|PubMed:21562494"
FT HELIX 4..23
FT /evidence="ECO:0007829|PDB:5YHF"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:5YHF"
FT TURN 37..40
FT /evidence="ECO:0007829|PDB:5YHF"
FT STRAND 43..49
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 51..53
FT /evidence="ECO:0007829|PDB:3AQO"
FT HELIX 56..73
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:3AQO"
FT TURN 84..86
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:3AQO"
FT HELIX 97..108
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 113..118
FT /evidence="ECO:0007829|PDB:3AQO"
FT HELIX 127..135
FT /evidence="ECO:0007829|PDB:3AQO"
FT HELIX 142..146
FT /evidence="ECO:0007829|PDB:3AQO"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 159..161
FT /evidence="ECO:0007829|PDB:3AQO"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 165..172
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:5YHF"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:3AQO"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:3AQO"
FT TURN 199..201
FT /evidence="ECO:0007829|PDB:5YHF"
FT STRAND 202..208
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 211..214
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 224..229
FT /evidence="ECO:0007829|PDB:3AQO"
FT HELIX 235..247
FT /evidence="ECO:0007829|PDB:3AQO"
FT STRAND 254..261
FT /evidence="ECO:0007829|PDB:3AQO"
FT HELIX 268..319
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 325..354
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 359..390
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 395..415
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 417..427
FT /evidence="ECO:0007829|PDB:5YHF"
FT TURN 445..447
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 448..469
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 475..478
FT /evidence="ECO:0007829|PDB:5YHF"
FT STRAND 480..487
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 493..502
FT /evidence="ECO:0007829|PDB:5YHF"
FT TURN 507..509
FT /evidence="ECO:0007829|PDB:5YHF"
FT STRAND 510..515
FT /evidence="ECO:0007829|PDB:5YHF"
FT STRAND 523..529
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 534..546
FT /evidence="ECO:0007829|PDB:5YHF"
FT STRAND 548..550
FT /evidence="ECO:0007829|PDB:3AQP"
FT STRAND 551..558
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 564..588
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 591..615
FT /evidence="ECO:0007829|PDB:5YHF"
FT STRAND 618..620
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 621..651
FT /evidence="ECO:0007829|PDB:5YHF"
FT TURN 652..654
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 657..689
FT /evidence="ECO:0007829|PDB:5YHF"
FT TURN 692..694
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 695..714
FT /evidence="ECO:0007829|PDB:5YHF"
FT HELIX 716..734
FT /evidence="ECO:0007829|PDB:5YHF"
SQ SEQUENCE 735 AA; 79678 MW; 6283A10A1163539D CRC64;
MNRKNLTSLF LLGVFLLALL FVWKPWAPEE PKVRLGLDLK GGLRIVLEAD VENPTLDDLE
KARTVLENRI NALGVAEPLI QIQGQKRIVV ELPGLSQADQ DRALKLIGQR AVLEFRIVKE
GATGTTVAQI NQALRENPRL NREELEKDLI KPEDLGPPLL TGADLADARA VFDQFGRPQV
SLTFTPEGAK KFEEVTRQNI GKRLAIVLDG RVYTAPVIRQ AITGGQAVIE GLSSVEEASE
IALVLRSGSL PVPLKVAEIR AIGPTLGQDA IQAGIRSALI GTLAIFLLIF AYYGPHLGLV
ASLGLLYTSA LILGLLSGLG ATLTLPGIAG LVLTLGAAVD GNVLSFERIK EELRAGKKLR
QAIPEGFRHS TLTIMDVNIA HLLAAAALYQ YATGPVRGFA VILAIGVVAS VFSNLVFSRH
LLERLADRGE IRPPMWLVDP RFNFMGPARY VTAATLLLAA LAAGVVFAKG FNYSIDFTGG
TAYTLRAEPN VEVETLRRFL EEKGFPGKEA VITQVQAPTA AYREFLVKLP PLSDERRLEL
ERLFASELKA TVLASETVGP AIGEELRRNA VMAVLVGLGL ILLYVAFRFD WTFGVASILA
VAHDVAIVAG MYSLLGLEFS IPTIAALLTI VGYSINDSIV VSDRIRENQK LLRHLPYAEL
VNRSINQTLS RTVMTSLTTL LPILALLFLG GSVLRDFALA IFVGIFVGTY SSIYVVSALV
VAWKNRRKAQ EASKA
