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Database: UniProt
Entry: K2GAV1_9BACI
LinkDB: K2GAV1_9BACI
Original site: K2GAV1_9BACI 
ID   K2GAV1_9BACI            Unreviewed;       761 AA.
AC   K2GAV1;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   25-OCT-2017, entry version 31.
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   ORFNames=MJ3_04454 {ECO:0000313|EMBL:EKE32193.1};
OS   Salimicrobium jeotgali.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Salimicrobium.
OX   NCBI_TaxID=1230341 {ECO:0000313|EMBL:EKE32193.1, ECO:0000313|Proteomes:UP000011746};
RN   [1] {ECO:0000313|EMBL:EKE32193.1, ECO:0000313|Proteomes:UP000011746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ3 {ECO:0000313|EMBL:EKE32193.1,
RC   ECO:0000313|Proteomes:UP000011746};
RX   PubMed=23144427; DOI=10.1128/JB.01808-12;
RA   Lee S.H., Jung J.Y., Jeon C.O.;
RT   "Draft Genome Sequence of Salimicrobium sp. Strain MJ3, Isolated from
RT   Myulchi-Jeot, Korean Fermented Seafood.";
RL   J. Bacteriol. 194:6695-6695(2012).
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: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_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}.
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:EKE32193.1}.
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DR   EMBL; AMPQ01000004; EKE32193.1; -; Genomic_DNA.
DR   RefSeq; WP_008588674.1; NZ_CP011361.2.
DR   EnsemblBacteria; EKE32193; EKE32193; MJ3_04454.
DR   KEGG; sje:AAV35_005135; -.
DR   PATRIC; fig|1230341.3.peg.924; -.
DR   KO; K12257; -.
DR   OrthoDB; POG091H02C5; -.
DR   Proteomes; UP000011746; 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_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000011746};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00284057};
KW   Protein transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425133};
KW   Reference proteome {ECO:0000313|Proteomes:UP000011746};
KW   Translocation {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425069};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425065};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425143};
KW   Transport {ECO:0000256|HAMAP-Rule:MF_01463,
KW   ECO:0000256|SAAS:SAAS00425109}.
FT   TRANSMEM    269    286       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    293    310       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    322    343       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    364    385       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    397    420       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    466    484       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    577    596       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    603    626       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    632    653       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    688    706       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    712    737       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   761 AA;  83459 MW;  182F88C1E22A1E19 CRC64;
     MKKRGRIVAF FLIVALLGTM IGTTVTGVAK DIKLGLDLQG GFEILYEVDP IDEEQEVNRQ
     VLEATVQSLT ERVDSLGISE ANINIEEPNR IRVQLAGVDN QQEARELLST TAELSFRDVE
     GNEYLDGSDI VEGSAQQSFD ANTNQPVVTV KMESAQEFYE VSDTITSKEQ DPETPYDDRM
     MVIWLDYNES ETTFPEEYGK EDPAYISALG FNNDEPIRST DVQIDGNFTV ESAKQLADML
     NAGSLPVNLE EMYSTSVGAQ FGEQAMNKTV IAGAIGIALI FLYMIAYYRF PGIIAAVTLS
     VYIYLILVVF ELMNGVLTLP GIAALILGVG MAVDANIITY ERIKEELKSG KSVMSAFKSG
     NKRSLATILD ANITTLIAAG VLFIFGTSSV KGFATMLIVS ILVSFITAVF GTRLFMGLWI
     HSRLLNKRPG WFGVKPSQIQ DINDTTPVNT TVKGKTFDFA GLRKRFFAIS IILIASGGIA
     LMIFKLNLGI DFTSGSRVSI LSDGNIKAPQ VEETLEEEFG VTPKQIVISG DNDEIAVARF
     ETVLPKDKVG EIQAHYEEKY GNTPNVSTVS PIVGQELAKN AALAVLYASI GIVIYVTIRF
     EFFFALTAIL ALLHDAFFII ALFSITRLEF DITIIAAILA IVGYSVNDTI VTFDRIRENL
     KLKRKVKTFG ELAKVVNESL MQTLARSFNT VITVVFAALM IFLFGASSIT NFGFALVVGL
     VAGTYSSLFI AAQLWLVMRG RTIEKKPIEY SAKKKTNGPQ V
//
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