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Database: UniProt
Entry: Q8Y703_LISMO
LinkDB: Q8Y703_LISMO
Original site: Q8Y703_LISMO 
ID   Q8Y703_LISMO            Unreviewed;       754 AA.
AC   Q8Y703;
DT   01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2002, sequence version 1.
DT   25-OCT-2017, entry version 98.
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=lmo1527 {ECO:0000313|EMBL:CAC99605.1};
OS   Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=169963 {ECO:0000313|EMBL:CAC99605.1, ECO:0000313|Proteomes:UP000000817};
RN   [1] {ECO:0000313|EMBL:CAC99605.1, ECO:0000313|Proteomes:UP000000817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-679 / EGD-e {ECO:0000313|Proteomes:UP000000817};
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A.,
RA   Baquero F., Berche P., Bloecker H., Brandt P., Chakraborty T.,
RA   Charbit A., Chetouani F., Couve E., de Daruvar A., Dehoux P.,
RA   Domann E., Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O.,
RA   Entian K.D., Fsihi H., Portillo F.G., Garrido P., Gautier L.,
RA   Goebel W., Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.M.,
RA   Kaerst U., Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E.,
RA   Maitournam A., Vicente J.M., Ng E., Nedjari H., Nordsiek G.,
RA   Novella S., de Pablos B., Perez-Diaz J.C., Purcell R., Remmel B.,
RA   Rose M., Schlueter T., Simoes N., Tierrez A., Vazquez-Boland J.A.,
RA   Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
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}.
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DR   EMBL; AL591979; CAC99605.1; -; Genomic_DNA.
DR   PIR; AG1265; AG1265.
DR   RefSeq; NP_465052.1; NC_003210.1.
DR   RefSeq; WP_003723531.1; NC_003210.1.
DR   ProteinModelPortal; Q8Y703; -.
DR   STRING; 169963.lmo1527; -.
DR   PaxDb; Q8Y703; -.
DR   EnsemblBacteria; CAC99605; CAC99605; CAC99605.
DR   GeneID; 987793; -.
DR   KEGG; lmo:lmo1527; -.
DR   PATRIC; fig|169963.11.peg.1568; -.
DR   eggNOG; ENOG4105C3D; Bacteria.
DR   eggNOG; COG0341; LUCA.
DR   eggNOG; COG0342; LUCA.
DR   HOGENOM; HOG000018636; -.
DR   KO; K12257; -.
DR   OMA; PNNQLVI; -.
DR   PhylomeDB; Q8Y703; -.
DR   Proteomes; UP000000817; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
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:0015031; P:protein transport; IBA:GO_Central.
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_01463,
KW   ECO:0000256|SAAS:SAAS00425060};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000817};
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:UP000000817};
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    259    277       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    353    375       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    381    405       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    455    474       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    570    587       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    594    615       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    677    695       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
FT   TRANSMEM    701    727       Helical. {ECO:0000256|HAMAP-Rule:
FT                                MF_01463}.
SQ   SEQUENCE   754 AA;  82615 MW;  F2BA633B501EB58B CRC64;
     MVKKSKIVIF FLVVAIIFGA VFGTAKMVMQ NINLGLDLQG GFEVLYEVSP ADGKGTVSKQ
     TLTDTVTSLD KRVNSLGVAE PSIQIEGNNR IRVQLAGVTD QAEARKMLST TAQLSFRDAN
     DKMMMNGSDL VAGGAKQAFD SSNNPIVTLK LKSADKFASV TKTILAEAPD NQLVIWLDWK
     EGQKYKTERE KKDPAYLSAP NVSSVLDTDK VEISGSFTTE EAKDLAELLN SGALPVKMKE
     VYSTSVGAQF GQDALQETIL AGIIGVIAIF IFMMAVYRLP GVIASITLVA YTYLVLLILS
     LLNATLTLPG IAGLILGIGM AVDANVITYE RIKEEIKVGR STKAAFEVGG KEAFRAILDG
     NLTTLIVAAV LFYFGTSSIK GFATVLIISI LVSFLTAVWG SRFLLGLLVK SNWLNNKPGF
     FAVKRKDIHN LHEGINSFSL KTHFDRFDFV KHHRLFLSIF AAIVIVGIVI LSIFRLNLGI
     DFASGTRAEV TANQTLTETQ IKKDLDTIDM PSDDIVFQGS GSKTAVVSYK GTLSQNDVAK
     FKNYFEDKYK HEPSISTVSP TVGKELAKNG FWALGVASVL IVLYIAVRFE FYMGIAAILS
     LLFDAFIIFI FFSVTRLEVD LTFIAAVLTV IGYSINDTIV TADRIRDISM KMQRFKTKEE
     IADAVNKALR QTFTRSINTI LTVIFTVLAL VLFGSESILN FSIALLVGLV SSVFSSIFMA
     MQLWYVFKAR QLRKKGPIST VKKKKPRNNG QPVV
//
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