ID A0A0K0TVD6_9RHIZ Unreviewed; 850 AA. AC A0A0K0TVD6; DT 11-NOV-2015, integrated into UniProtKB/TrEMBL. DT 11-NOV-2015, sequence version 1. DT 27-SEP-2017, entry version 15. 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:0000313|EMBL:AKR55606.1}; GN Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463}, secF GN {ECO:0000256|HAMAP-Rule:MF_01464}; GN ORFNames=XM25_07275 {ECO:0000313|EMBL:AKR55606.1}; OS Devosia sp. H5989. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Hyphomicrobiaceae; Devosia. OX NCBI_TaxID=1643450 {ECO:0000313|EMBL:AKR55606.1, ECO:0000313|Proteomes:UP000037066}; RN [1] {ECO:0000313|EMBL:AKR55606.1, ECO:0000313|Proteomes:UP000037066} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=H5989 {ECO:0000313|EMBL:AKR55606.1, RC ECO:0000313|Proteomes:UP000037066}; RX PubMed=26337876; RA Nicholson A.C., Whitney A.M., Humrighouse B., Emery B., Loparev V., RA McQuiston J.R.; RT "Complete Genome Sequence of Strain H5989 of a Novel Devosia RT Species."; RL Genome 3:e00934-15(2015). 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-YajC and YidC. {ECO:0000256|HAMAP- CC 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-YajC and YidC. {ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP011300; AKR55606.1; -; Genomic_DNA. DR RefSeq; WP_049705224.1; NZ_CP011300.1. DR EnsemblBacteria; AKR55606; AKR55606; XM25_07275. DR KEGG; deq:XM25_07275; -. DR PATRIC; fig|1643450.3.peg.1476; -. DR KO; K12257; -. DR Proteomes; UP000037066; 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 InterPro; IPR000731; SSD. 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. DR PROSITE; PS50156; SSD; 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:UP000037066}; 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:UP000037066}; 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 368 388 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 395 417 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 423 445 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 466 487 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 499 522 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 549 569 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 668 689 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 696 717 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 723 744 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 765 791 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT TRANSMEM 803 827 Helical. {ECO:0000256|HAMAP-Rule: FT MF_01464}. FT DOMAIN 692 824 SSD. {ECO:0000259|PROSITE:PS50156}. SQ SEQUENCE 850 AA; 90949 MW; E7920664511D9986 CRC64; MQFSPIRAVI IAIVAILAVA FTIPSFLPKD TLDAMPDWMP KRTIVLGLDL QGGSHLLLGV NKQSIVDQRV KDLRRDARAV LANENGIGNI ITTGTQSITV ELTDPTQQDA ALKALETLQN NISNTMFSVG GTPELSFSTT SDGKITVALT DEGINQRMSS LVTQSMEVIR KRVDELGTTE PSIQRQGSDR VLLQVPGFGD STRLKDIVSK TARLTFHMVY PGMTAAQAEA QGLPAGTIIL PSQDGGKELL YEDVSLGGES LVDSQPGFDQ QTGRSVVTFK FDTRGAVTFS DITSKNVGKR FAIVLDNQVL TAPVIQQPIT GGSGQISGNF TPQSAQDLAV LLRAGALPAS LDIIEERTVG PSLGADSIRA GLIAGAVAAA AVILFMLMAY GLWGVFANIS LILNIFVMLG SLSMLGATLT LPGIAGIILT IGMAVDANVL IYERIREEQQ AGRSNLQAIT AGFERAWGTI VDSHLTSLIA AIVLFFLGSG PVQGFAVTLA LGILTSMFTA YTVTLFIAGI WYRRRRPKTV QIRLIHFIPD HTKIPFMKFA RPAIIISVLA IAGSMGSFFT KGMNLGIDFT GGSAIEVQHV GGPADPGDIR QRLSELGLGE IQVQGFGTPE DVLIRVQAQE GGDAAQQAAV QKVRDALQSG GYEVRRTESV GPSVSGELAV SGAIGLGVAL LAIMVYVWFR FEWQYAVGAI VSTFHDVLLT IGFFSITGIE FNLTSIAAIL TIVGYSLNDT VVVYDRVREN LRKYKKMSLP ELIDLSINST LARTTLTAFT TLLALIPLVL FGGEVIRSFT ISMTWGVLIG TYSSIVIAAP ILIWFGLRAR ADQAKDEKQA KEKRADGAAV //