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Database: UniProt
Entry: A0A1B9Y001_9FLAO
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ID   A0A1B9Y001_9FLAO        Unreviewed;       992 AA.
AC   A0A1B9Y001;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, 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=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   ORFNames=BA195_00040 {ECO:0000313|EMBL:OCK43134.1};
OS   Tenacibaculum soleae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Tenacibaculum.
OX   NCBI_TaxID=447689 {ECO:0000313|EMBL:OCK43134.1, ECO:0000313|Proteomes:UP000093186};
RN   [1] {ECO:0000313|EMBL:OCK43134.1, ECO:0000313|Proteomes:UP000093186}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-KL19 {ECO:0000313|EMBL:OCK43134.1,
RC   ECO:0000313|Proteomes:UP000093186};
RA   Eisen J.A., Coil D.A., Lujan K.M.;
RT   "Draft Genome Sequence of Tenacibaculum soleae UCD-KL19.";
RL   Submitted (JUN-2016) 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:OCK43134.1}.
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DR   EMBL; MAKX01000001; OCK43134.1; -; Genomic_DNA.
DR   RefSeq; WP_068701175.1; NZ_MAKX01000001.1.
DR   AlphaFoldDB; A0A1B9Y001; -.
DR   STRING; 447689.BA195_00040; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000093186; 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; 1.
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; 2.
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:UP000093186};
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        505..523
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        530..548
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        554..577
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        598..625
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        631..655
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        689..710
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        825..843
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        850..876
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        882..899
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        935..953
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        959..983
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          192..249
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          486..652
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   DOMAIN          808..985
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   992 AA;  108572 MW;  B6EFF6B409952310 CRC64;
     MQNKGLIKLF AVLFGLVSLY QLSFTFFANK VEDNAKVYAK ENVKDNNGRA LAKFERKYLD
     SVANNEVVNL GVSKYTYNDI KEREMNLGLD LKGGINAILQ VSVKDILVAL ANDSNNTVFR
     KALANANEAQ KASQDNYLDL FFNEFETLSN GSVKLSDPAI FGTKSLREKI DFNKTNAEVK
     EVLQEEINTS INTSFEVLRS RIDKFGVTQP SIQRIGTSGR IQIELAGAKD IERVTKLITS
     TAELQFWEVY TNAEIQNFFF AANAKVAELL KDDSTTKVAK DSTKADDIDD LLGETADSTK
     VENQKNLFTY LFPNVAQNQQ QMSSLVAQAK VQDTAKVNSL LANKSVRALL PANLKYVKFL
     WDYKAQTGAD GSAEIIGLYA IKSNRNDKAA IDGDVIADAK QDFNEVSKPV VSMSMNGVGS
     KKWAKLTGDN TGRFVAVVLD DYVYTAPSVP GAITGGQTQI SGGSMTVEEA QDIATVLKAG
     KLPAPARIIQ MEVVGPSLGQ ESIDASIWSF GLAIFLILIW MVLYYGKAGL FSNIALLVNI
     LFIFGWLVSF NAVLTLPGIA GIILTIGMSV DANVIIFERI KEALRGGKDL NTAVSEGFSF
     KGALSAIIDA NITTFLTGLI LFVFGTGPIK GFAYTLMLGI ATSLFTAIFI TRLFIDSTVN
     KGTNLTFNTK ISKNWFNNIN IEFLKKRKLA YIISGFFILV GLISIFTLGL KQGVDFKGGR
     SYVVRFDQAM NATEVASSLQ GAFEAAPEVK TYGSDHQLKI TTTFKIDEEG TEVDEQVQNA
     LYTGLKSYLG TTSYEDFKPG FEKVGSGIMS YMKVEPTIAD DIKKSALWAV IGSLLVVFLY
     ILLRFRKMSY SIGAVSAVFH DVLVVLGVFS ICYKFMPFDM EIGQSFIAAI LTVVGYSLND
     TVVIFDRIRE YADNSNSLTA GLVDKALSST LGRTINTSLT TLLVMLAIFF FGGDSIKGFM
     FALIVGVVVG TYSSLFVATP IMFDSSKKEE KK
//
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