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
//