(data stored in ACNUC7421 zone)

SWISSPROT: Q47SZ2_THEFY

ID   Q47SZ2_THEFY            Unreviewed;       911 AA.
AC   Q47SZ2;
DT   13-SEP-2005, integrated into UniProtKB/TrEMBL.
DT   13-SEP-2005, sequence version 1.
DT   08-MAY-2019, entry version 100.
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=Tfu_0387 {ECO:0000313|EMBL:AAZ54425.1};
OS   Thermobifida fusca (strain YX).
OC   Bacteria; Actinobacteria; Streptosporangiales; Nocardiopsaceae;
OC   Thermobifida.
OX   NCBI_TaxID=269800 {ECO:0000313|EMBL:AAZ54425.1, ECO:0000313|Proteomes:UP000000434};
RN   [1] {ECO:0000313|Proteomes:UP000000434}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YX {ECO:0000313|Proteomes:UP000000434};
RX   PubMed=17209016; DOI=10.1128/JB.01899-06;
RA   Lykidis A., Mavromatis K., Ivanova N., Anderson I., Land M.,
RA   DiBartolo G., Martinez M., Lapidus A., Lucas S., Copeland A.,
RA   Richardson P., Wilson D.B., Kyrpides N.;
RT   "Genome sequence and analysis of the soil cellulolytic actinomycete
RT   Thermobifida fusca YX.";
RL   J. Bacteriol. 189:2477-2486(2007).
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. SecDF uses the
CC       proton motive force (PMF) to complete protein translocation after
CC       the ATP-dependent function of SecA. {ECO:0000256|HAMAP-
CC       Rule:MF_01463, ECO:0000256|SAAS:SAAS01082309}.
CC   -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec
CC       protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary 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
CC       protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}.
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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP000088; AAZ54425.1; -; Genomic_DNA.
DR   RefSeq; WP_011290834.1; NC_007333.1.
DR   STRING; 269800.Tfu_0387; -.
DR   EnsemblBacteria; AAZ54425; AAZ54425; Tfu_0387.
DR   KEGG; tfu:Tfu_0387; -.
DR   eggNOG; ENOG4107RSV; Bacteria.
DR   eggNOG; COG0341; LUCA.
DR   eggNOG; COG0342; LUCA.
DR   HOGENOM; HOG000018636; -.
DR   KO; K12257; -.
DR   OMA; FEWPFAV; -.
DR   BioCyc; TFUS269800:G1G4Q-391-MONOMER; -.
DR   Proteomes; UP000000434; 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: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: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   PANTHER; PTHR30081; PTHR30081; 3.
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   3: Inferred from homology;
DR   PRODOM; Q47SZ2.
DR   SWISS-2DPAGE; Q47SZ2.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082273};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000434};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082292};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082319};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000434};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082267};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082280};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082333};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS01082300}.
FT   TRANSMEM     12     31       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    332    350       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    357    379       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    385    404       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    465    487       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    493    517       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    529    549       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    555    577       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    609    627       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    723    740       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    747    768       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    774    795       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    826    844       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    850    876       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   911 AA;  96943 MW;  88C6A69F66D8C4A2 CRC64;
     MTSSPGSGAR WLRALISLLI MAGAFTAGWF LKPKLGLDLS GGTQIVLETR DAEDGTKANA
     SNTDLVVEVL RNRIDSLGVS EATLSRSGEN RIIVELPGVQ DPTEAAEVLG QTAQLTIHPV
     LGVDQSIGTT GGGMFGDFRN APADNSAEAS DSEAQEEESP AEDEEGSEES TESGEEAEAV
     DPEDIALTLP DESGTLLQLG KPALTGDQVD RAEATLNELQ TEWLVNVEFK GAGREAWKKL
     TGEAACHSPG DPRRRIAIVL DNEIISAPEV DANDVACNVG MSGGRTSITG GFDAEEAKEL
     ALLIEGGSLP LPVEEVQRQT VGPTLGAEAI KASFIAGLIG IALTAIYISI SYRFAGFLAS
     VALLCYTVIA YAALVALGAT LTLPGLAGFV LSIGMAIDAN VLIFERTREE YQRQEKVYQA
     NKSAGMLDAT EKEQDEAAAG VVTRRRRRAI PPNLLKSFTV GSQRAWSAVL DTNITTLIAA
     VLLFFLASGT VQGFGVTLGL GTIASMISAL LIARVLMEWT VSRFTPLRRL WLIGAAAVVV
     GLVAVLSDGL RVDNVLLLVS GALGVLAVSV AIIPLIVRKF PRSSGIAHIS AVRKWLVEHN
     PDLMKRSTLW LGITGVVTVL ALLGFAVRSP NLGVEFTGGR VMTFSVTEEL NADQARELVA
     GAGYANAVVQ EVEGGEISVR TGHISDQEAA KIQDALAEEG GEVERTSDEK IGPSMGSELR
     NKALIALIVA LVLQMAYLAW RFRWSFGLAT MLALAFDIIL VIGLFVWLGK PIDGVFLAAL
     LSIIGFSVND SVVVFDRVRD EWAHKPKGDF REIANSSVLH TLPRTVNSGI GGLFILAALA
     VLGGSSLTDF SIAMLVGLIS GIFSTVFVAV PLAIWLQRFD RTPPPHEVKE RKTKQRKQQR
     AIRERTDGAV V
//

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