ID A0A0E9N2R9_9BACT Unreviewed; 1038 AA.
AC A0A0E9N2R9;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=secDF {ECO:0000313|EMBL:GAO44307.1};
GN Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463}, secF
GN {ECO:0000256|HAMAP-Rule:MF_01464};
GN ORFNames=FPE01S_03_03450 {ECO:0000313|EMBL:GAO44307.1};
OS Flavihumibacter petaseus NBRC 106054.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Flavihumibacter.
OX NCBI_TaxID=1220578 {ECO:0000313|EMBL:GAO44307.1, ECO:0000313|Proteomes:UP000033121};
RN [1] {ECO:0000313|EMBL:GAO44307.1, ECO:0000313|Proteomes:UP000033121}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 106054 {ECO:0000313|EMBL:GAO44307.1,
RC ECO:0000313|Proteomes:UP000033121};
RA Miyazawa S., Hosoyama A., Hashimoto M., Noguchi M., Tsuchikane K., Ohji S.,
RA Yamazoe A., Ichikawa N., Kimura A., Fujita N.;
RT "Whole genome shotgun sequence of Flavihumibacter petaseus NBRC 106054.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAO44307.1}.
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DR EMBL; BBWV01000003; GAO44307.1; -; Genomic_DNA.
DR RefSeq; WP_046370250.1; NZ_BBWV01000003.1.
DR AlphaFoldDB; A0A0E9N2R9; -.
DR STRING; 1220578.FPE01S_03_03450; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000033121; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015450; F:protein-transporting ATPase 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 Gene3D; 3.30.1360.200; -; 1.
DR Gene3D; 3.30.70.3220; -; 1.
DR Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
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; IPR048631; SecD_1st.
DR InterPro; IPR048634; SecD_SecF_C.
DR InterPro; IPR005665; SecF_bac.
DR NCBIfam; TIGR00916; 2A0604s01; 2.
DR NCBIfam; TIGR01129; secD; 1.
DR NCBIfam; TIGR00966; transloc_SecF; 1.
DR PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF21760; SecD_1st; 1.
DR Pfam; PF02355; SecD_SecF; 2.
DR PRINTS; PR01755; SECFTRNLCASE.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
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:UP000033121};
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 539..558
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 563..583
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 589..613
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 634..655
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 661..685
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 720..740
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 850..868
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 875..897
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 909..930
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 961..979
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 985..1009
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 202..260
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 516..689
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 828..1013
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 1038 AA; 114011 MW; A89BD689F8730677 CRC64;
MRSLVSIFAA ILILISLYQL SFTWFVNKHE KAIEEKARKY VSAIPTPEQK YPGNNELQAA
YRDSLAEIKK DRVRQLQDST RNEKITWWGH TYQKAKESEL LLGLDLQGGI NVTMDVALDG
LIRGLSNNPQ DANLKKAIEE ALKRKVNSDA DFITLFSQSF RDVNPGAKMA PLFANSSRNK
LKIDASDESV IAYIRDQANA AMKQTYDVLT KRIDKFGVAQ PNISLDENKG IITVELAGAT
DPERVRKYLQ SSANLQFFEV YNIGELDKSL EAADKELALL LKGGDTSKAA VIDTTKSAAA
GDTTNKSLAD VLKGNKDTSK TAMAAKSAEE VRKDHPLLAS ISFVTPQDAN KDGRPEFAPY
LGFVPTKDTN LVSSYLHNPA VTNNMPGDVK FLYGMPEKDK DGKELDFVPL YAIKKQQGTE
KAKLEGEYIT DAFQDFNSLT NQVTVNMVMN KQGEKIWAKM TGDNVGRAIA IVLDDIVYSA
PNVNEPITGG NSQISGSFSV QEGQDLSNIL KSGKLDAPAK IVQETVVGPT LGQEAVKGGT
LAFIIAFAII FVLMLVYYNT AGWVANIALI LNLLFTIGVL SALNATLTAP GIAGLVLTIG
MAVDTNVIIF ERIKDELTRG KSYQQAVNDG YRRSLAPVLD GHITTLLTAI ILFYFGLGPV
LGFATTQILG ILLSLFCGIL VSRLITDFYT NKNRHFNYFT NLSRSIFKHA KYNFVQYRKV
TYIISGVVLL LGIAAIFNGF NEGVEFSGGR SYIVKFPNAV KQQEVGDALD KVFGKYPVIK
TYGGPTQLDI TTDYMVEQTS PEADAKVQAT LFEGLKPFLP ANTTPEVFNT KYKQASKRVD
PTISDDLKAG AKWATFWSLL AIALYIFIRF RDWRYSLGTI VALLHDVLVT LAVFSFFKNI
VPFPLEIDQH FIAAILTVIG FSMNDTVIVF DRVRENSHLM KGASKAEIIN KSINDTLTRT
IMTSVTVFLT ILVLFLVGGE VTKGFAFAML IGVFTGCYSS IFVAAPILVD FAKDRPLGES
KIETATSSTT NNTAVAKG
//
