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Database: UniProt
Entry: N4W9Z1_9BACI
LinkDB: N4W9Z1_9BACI
Original site: N4W9Z1_9BACI 
ID   N4W9Z1_9BACI            Unreviewed;       753 AA.
AC   N4W9Z1;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   23-MAY-2018, entry version 30.
DE   SubName: Full=Bifunctional preprotein translocase subunit SecD/SecF {ECO:0000313|EMBL:ENH97093.1};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=J416_07387 {ECO:0000313|EMBL:ENH97093.1};
OS   Gracilibacillus halophilus YIM-C55.5.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae;
OC   Gracilibacillus.
OX   NCBI_TaxID=1308866 {ECO:0000313|EMBL:ENH97093.1, ECO:0000313|Proteomes:UP000012283};
RN   [1] {ECO:0000313|EMBL:ENH97093.1, ECO:0000313|Proteomes:UP000012283}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM-C55.5 {ECO:0000313|EMBL:ENH97093.1,
RC   ECO:0000313|Proteomes:UP000012283};
RA   Sugumar T., Polireddy D.R., Antony A., Madhava Y.R., Sivakumar N.;
RT   "Draft genome sequence of Gracibacillus halophilus YIM-C55.5, a
RT   moderately halophilic and thermophilic organism from the Xiaochaidamu
RT   salt lake.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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_01464, ECO:0000256|SAAS:SAAS00541769}.
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_01464}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01464}.
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_01464}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:ENH97093.1}.
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DR   EMBL; APML01000023; ENH97093.1; -; Genomic_DNA.
DR   RefSeq; WP_003467432.1; NZ_APML01000023.1.
DR   EnsemblBacteria; ENH97093; ENH97093; J416_07387.
DR   PATRIC; fig|1308866.3.peg.1493; -.
DR   OrthoDB; POG091H02C5; -.
DR   Proteomes; UP000012283; Unassembled WGS sequence.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
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   Pfam; PF07549; Sec_GG; 1.
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;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000012283};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000012283};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM    261    278       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    285    302       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    314    335       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    356    378       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    384    412       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    458    478       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    569    590       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    597    618       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    624    645       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    680    701       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    707    730       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
SQ   SEQUENCE   753 AA;  83634 MW;  81E967F4BF93FC35 CRC64;
     MVKKGRIIAF FLIVIILGAT IGTTYTNIAK NINLGLDLQG GFEVLYTAET IEDGEEVTTK
     NLESTTQILR ERVDSLGISE PRFNIEEPNR IRVQLPGVED QEEARDLLST SASLSFRDVN
     DKEYLDGSDI VNGSAQQDFS QDTNQPIVTV QFKDADRFGD ATREIMNDQD LTNQIVIWMD
     YEEGDSYQEE VQKEDPKFIS APTFTDVLQN KSIQIEGPDF TVDSAQRLAD ILNAGSLPVN
     LEEEYSRSVG AQFGQQALDK TIFASVIGII LIFAYMILYY RFPGMIAAIT LSIYVYLVLL
     VFELMNGVLT LPGIAALVLG VGMAVDANII TYERIKEELK EGKSIKAAFR TGNQHSLSTI
     IDANITTLIA AAVLFIFGTS SVKGFATLLI VSIVLSFVTA VFGSRLFLGF WVNSHFLNKR
     PGFFGVKKHQ IKDINSKEEV QPTVFGRQFD FVGHRKKFFR LSLFLVALGI ICLAVFRLNL
     GIDFVSGSRI EVLADRSLTT EEIENAYDEL GMEPSTQVAI QGDDDHIAVT RFEDDLSKDK
     IAEVQNYFEE KYGNTPTVNT VSPIVGQELA QNAILAVLYA SIGIIIYVTI RFEFYSALTA
     ILALLHDAFF IVALFAITRI EFDITIIAAI LTIVGYSIND TIVTFDRIRE NMKKEKRIKS
     FAKLAGIINR SLMQTLARSI NTVLTVIFAA TMLLIFGASA ITNFSFALVV GLLAGTYSSL
     FIAAQVWLAW RGKTVDEKPI DYREKKANDG PQV
//
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