ID A0A0U3AGC0_9FLAO Unreviewed; 1005 AA. AC A0A0U3AGC0; DT 16-MAR-2016, integrated into UniProtKB/TrEMBL. DT 16-MAR-2016, sequence version 1. DT 12-AUG-2020, entry version 24. 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=AUW17_10610 {ECO:0000313|EMBL:ALU75675.1}; OS Tenacibaculum dicentrarchi. OC Bacteria; Bacteroidetes; Flavobacteriia; Flavobacteriales; OC Flavobacteriaceae; Tenacibaculum. OX NCBI_TaxID=669041 {ECO:0000313|EMBL:ALU75675.1, ECO:0000313|Proteomes:UP000061908}; RN [1] {ECO:0000313|EMBL:ALU75675.1, ECO:0000313|Proteomes:UP000061908} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AY7486TD {ECO:0000313|EMBL:ALU75675.1, RC ECO:0000313|Proteomes:UP000061908}; RX PubMed=26893432; RA Grothusen H., Castillo A., Henriquez P., Navas E., Bohle H., Araya C., RA Bustamante F., Bustos P., Mancilla M.; RT "First Complete Genome Sequence of Tenacibaculum dicentrarchi, an Emerging RT Bacterial Pathogen of Salmonids."; RL Genome Announc. 4:e01756-15(2016). CC -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with CC the SecYEG preprotein conducting channel. SecDF uses the proton motive CC force (PMF) to complete protein translocation after the ATP-dependent CC function of SecA. {ECO:0000256|HAMAP-Rule:MF_01463}. CC -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec protein CC translocation apparatus which comprises SecA, SecYEG and auxiliary CC 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 protein CC translocation apparatus which comprises SecA, SecYEG and auxiliary CC proteins SecDF. Other proteins may also be involved. CC {ECO:0000256|HAMAP-Rule:MF_01463}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01463}; CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01463}. Membrane CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein CC {ECO:0000256|ARBA:ARBA00004141}. 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 of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}. 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; CP013671; ALU75675.1; -; Genomic_DNA. DR RefSeq; WP_058885815.1; NZ_CP013671.1. DR EnsemblBacteria; ALU75675; ALU75675; AUW17_10610. DR KEGG; tdi:AUW17_10610; -. DR KO; K12257; -. DR OrthoDB; 410730at2; -. DR Proteomes; UP000061908; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. 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 PANTHER; PTHR30081; PTHR30081; 3. DR Pfam; PF07549; Sec_GG; 2. DR Pfam; PF02355; SecD_SecF; 2. DR PRINTS; PR01755; SECFTRNLCASE. DR TIGRFAMs; TIGR00916; 2A0604s01; 1. DR TIGRFAMs; TIGR00966; 3a0501s07; 1. DR TIGRFAMs; TIGR01129; secD; 1. PE 3: Inferred from homology; KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP- KW Rule:MF_01463}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01463}; KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP- KW Rule:MF_01463}; Reference proteome {ECO:0000313|Proteomes:UP000061908}; KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP- KW Rule:MF_01463}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_01463}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_01463}; KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01463}. FT TRANSMEM 508..526 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 533..551 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 557..580 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 601..628 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 634..658 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 692..713 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 828..846 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 853..879 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 885..908 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 938..956 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" FT TRANSMEM 962..986 FT /note="Helical" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463" SQ SEQUENCE 1005 AA; 109874 MW; AFDD878DCE1A9825 CRC64; MQNKGLIKLF AVLFGLVSLY QLSFTFFANK VEDSAKVYAK ENAKGNSGRE LAKFERKYLD SVANDQVVNL GIGKYSYNDI KEREMNLGLD LKGGINAILQ VSVKDILIAL ANNSENTVFR SALAKANEAQ KDSQENYLDL FLTQFETLSN GSIKLSDPAI FGTKSLREKI DFNKTNAQVK EVLQQEINSS INTSFEVLRS RIDKFGVTQP NIQRIGNSGR IQIELPGAKD IERVTKLITS TAELQFWEVY TNAEVQNFFF SANAKVAELL KDDSITATTQ VKDSAKADDI DDLLGTSTDA AVKANTQKNL FTYLYPNVAQ NQQQMSSLVA QAKVQDTAQV NSLLAHKSVQ ALLPANLKYV KFLWDYKAQK SADGTAEIIG LYAIKSNRND KATIDGDVIS DANQDFDQLS KPVVSMTMNA SGTKKWAKMT GDNVGKFVAV VLDNYVYTAP VVNGAITGGS TQISGGTMTV EEAQDISTVL KAGKLPAPAR IIQAEVVGPS LGQESINASI WSFGLAILLI LVWMFLYYGK AGIYANIALL VNILFIFGWL ASYNAVLTLP GIAGIILTIG MSVDANVIIF ERIKEALRGG QTLETAVDEG FSFKGALSAI IDANITTFLT GVILFIFGTG PIKGFAYTLM LGIATSLFTA IFITRLFIDK SIEKGTGLPF NTSISKNWFQ NINIEFLKKR KLAYIVSGFF ILAGLVSIFT LGLKQGVDFK GGRSYVVRFD QPMNATQVAT SLKDAFKSAP EVKTYGSDHQ LKITTAFKID EDGSEVDEIV QKSLFTGLKA YLGTTSYEDF KPGFEKAGSG IMSYMKVEPT IADDIKKSAL WAVIGSLIVV FLYILLRFRK IAFSIGAVVA VFHDVLVVLG VFSICYKFMP FDMEIGQSFI AAILTVVGYS LNDTVVIFDR IREFTQEKTT ISASLVNKAL NSTLGRTINT SLTTLLVMLA IFFFGGDSIK GFMFALIVGV VVGTYSSLFV ATPIMFDASK KAEAVKEQEE NQEIA //