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Database: UniProt
Entry: G2NQ31_STREK
LinkDB: G2NQ31_STREK
Original site: G2NQ31_STREK 
ID   G2NQ31_STREK            Unreviewed;       775 AA.
AC   G2NQ31;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   23-MAY-2018, entry version 51.
DE   SubName: Full=Protein-export membrane protein SecD {ECO:0000313|EMBL:AEN13512.1};
GN   Name=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   ORFNames=SACTE_5723 {ECO:0000313|EMBL:AEN13512.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN13512.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN13512.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C.,
RA   Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I.,
RA   Adams A., Raffa K., Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) 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}.
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DR   EMBL; CP002993; AEN13512.1; -; Genomic_DNA.
DR   RefSeq; WP_014049462.1; NC_015953.1.
DR   STRING; 862751.SACTE_5723; -.
DR   EnsemblBacteria; AEN13512; AEN13512; SACTE_5723.
DR   KEGG; ssx:SACTE_5723; -.
DR   PATRIC; fig|862751.12.peg.5937; -.
DR   eggNOG; ENOG4105C3D; Bacteria.
DR   eggNOG; COG0341; LUCA.
DR   eggNOG; COG0342; LUCA.
DR   KO; K12257; -.
DR   OrthoDB; POG091H02C5; -.
DR   BioCyc; SSP862751:G1GPM-5791-MONOMER; -.
DR   Proteomes; UP000001397; Chromosome.
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; 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;
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001397};
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:UP000001397};
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      6     24       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    305    330       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    336    355       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    376    403       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    409    432       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    475    495       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    612    633       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    639    660       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    691    709       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
FT   TRANSMEM    715    741       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01464}.
SQ   SEQUENCE   775 AA;  80676 MW;  FCBA7AF11BC628F9 CRC64;
     MTRATAVRAV LAAAVLLVSV YITLTMSPRL GLDLQGGTRM VLQAKDSDTA TADRDSTDRT
     LEVLRQRVDS LGVAEPTLTR SGEDRIIVEL PDVQDPRQAA EVLGKTAQLS FHPVQGPGTE
     PAADDKEKDE GEGSKAGPTL PDEQGDLLAL GPVRLSGAGV KDATASFDAQ QGTGWSVSLD
     FHKDAGKKWT GLTGEAACNP VQDERRRVAI VLDGKVISSP QVSPSVGCNV GLPSGSTQIT
     GSFGADEARD LALLIKGGSL PVPVEIVEQR IVGPTLGAAA IDASARAALI GAAATALFIT
     VMYRLFGALA ALALAAYGVI SYAALVVLGV TLTLPGLAGF VLAIGMAVDA NVLVFERARE
     ECADRPNRTL LSALTAGFRG AWSAVADSNV TTLIAAGLLF FLGSGPVKGF GVTLAIGVIA
     SMFSALVIAR ALTEIAAGSR FVSGYRGVNG IARPGAVRTR LNARDPQLFR SPRRWLAFSA
     VLVAVAVAGI VVRGVNLGVE FTGGRLVEYS TSRPVDVEKA RDALSTAGFG DAEVTTAGDG
     DLSVRTGKLD DDGERAVRAA LAEEGGEATK IRDELIGPSL GDELRRNALI ALGVAVFVQL
     AYLAARFRWT FAVASVGALV HDVIILVGAF AWLGRTVDGI FLAALLTVIG YSVNDSVVVF
     DRVRELWAKS RRTPLPDIAN RAVLQTVPRT VNTGMGALFI LAALAVLGGD SLADFALALL
     IGICVGTYSS VMTAVPGALL LETSSKAPPP ARKRAPGRKV SRQQRRDPLD NGARV
//
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