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Database: UniProt
Entry: A0A2I9E503_9FLAO
LinkDB: A0A2I9E503_9FLAO
Original site: A0A2I9E503_9FLAO 
ID   A0A2I9E503_9FLAO        Unreviewed;       987 AA.
AC   A0A2I9E503;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 26.
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=C21_01668 {ECO:0000313|EMBL:GBF19502.1};
OS   Arenibacter sp. NBRC 103722.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Arenibacter.
OX   NCBI_TaxID=1113929 {ECO:0000313|EMBL:GBF19502.1, ECO:0000313|Proteomes:UP000095208};
RN   [1] {ECO:0000313|EMBL:GBF19502.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C-21 {ECO:0000313|EMBL:GBF19502.1};
RA   Ito K., Nakajima N., Yamamura S., Tomita M., Suzuki H., Amachi S.;
RT   "Draft Genome Sequence of Arenibacter sp. Strain C-21, an Iodine-
RT   Accumulating Bacterium Isolated from Surface Marine Sediment.";
RL   Genome Announc. 4:e01155-16(2016).
RN   [2] {ECO:0000313|EMBL:GBF19502.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=C-21 {ECO:0000313|EMBL:GBF19502.1};
RA   Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL   Submitted (JAN-2018) 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:GBF19502.1}.
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DR   EMBL; BDGL02000006; GBF19502.1; -; Genomic_DNA.
DR   RefSeq; WP_031442773.1; NZ_BDGL02000006.1.
DR   AlphaFoldDB; A0A2I9E503; -.
DR   Proteomes; UP000095208; 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; 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:UP000095208};
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        497..514
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        521..541
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        547..568
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        625..644
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        679..696
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        817..834
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        841..864
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        876..896
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        926..944
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        950..974
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          192..246
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          475..647
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   DOMAIN          796..976
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   987 AA;  107792 MW;  BBD95B84B99FB4EC CRC64;
     MQNKGLIKLF AFLFGLVSIY QLSYTFITNK VEKDATVFAT NKISESEEDY LAKREALEAR
     YLDSIGGNSI LGFTNYDEAK KKELNKGLDL KGGINVTLQI SVKDILKGLA NNTKNPVFNK
     ALADADAASK SSDATYIDLF FESFDKIKGD TKLASPDIFA NKGLSDVINF QMTDDQVKPI
     IRTKIDESIV SAFEVLRERI DGFGVTQPNI QREGNSGRIL VELPGARDIG RAQDLLSSTA
     QLEFWETYKQ SNPSLSTFLQ AANERLKTLV EVEKPEEVVK PESELDSLLS DVAQDSLDFS
     QDVNPLFSLL IPANPNGNAL VSAAIQDTAK IGEYLRMKEI RRLIPADIQF VKFVWERPTE
     GSEVVELYAL KSNRDNTPRI SGDVVSDASD TFDQYNKPAV TMTMNTKGAK EWEKLTGDAF
     NNQTGIAIVL DNKVYTAPGV SSGPISGGRS EITGTFTINE TKDIANVLRA GKLPASAEII
     QSEIVGPSLG QEAINSGFFS FMIAMAIVLV WMVFYYGKAG IFADIALLLN ILLIFGVLVS
     LNAVLTLPGI AGIVLTIGMS VDANVLIFER IKEELAKGKG QSQAIADGFG NALSSILDAN
     ITTGLTALIL FVFGSGPIKG FATTLLIGIV TSLFTAIFIT RLLVDWYVSG KGRKLDFSTA
     MTKNLFKNIN INFLAKRKIA YIASSILVAI GLFSLLTQGL QQGVDFVGGR SYTVRFEKMV
     NPSEIASELN TVFGSGTNVK TYGEANQIKI TTPYKVDVEG IEVDNEIQNK LYASLQKYLP
     DGTSFEDFTI GSGEKSIGIL QSVKVGPTIA DDIKKNAFLA IIGSLAVVFL YILFRFRRWQ
     FSLGAVAAVF HDILIVLGVF SIFGKLMPFN MEIDQAFIAA ILTVIGYSLN DTVVVFDRIR
     EIIAEKGWKA GENTNLALNS TLSRTLNTSM TTLVVLLAIF IFGGESLRGF MFAMIIGIIV
     GTYSSLFIAT PVMFDTLKKK TQIGKEE
//
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