ID A0A258WYE3_9SPHI Unreviewed; 984 AA.
AC A0A258WYE3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
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=B7Y24_02460 {ECO:0000313|EMBL:OYZ33200.1};
OS Sphingobacteriales bacterium 16-39-50.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1970581 {ECO:0000313|EMBL:OYZ33200.1, ECO:0000313|Proteomes:UP000216983};
RN [1] {ECO:0000313|EMBL:OYZ33200.1, ECO:0000313|Proteomes:UP000216983}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16-39-50 {ECO:0000313|EMBL:OYZ33200.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OYZ33200.1}.
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DR EMBL; NCHA01000001; OYZ33200.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A258WYE3; -.
DR Proteomes; UP000216983; 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; 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};
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 501..526
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 533..556
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 562..583
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 604..625
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 631..656
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 691..711
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 812..830
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 837..859
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 871..892
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 925..943
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 949..973
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 181..235
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 489..659
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 785..976
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 984 AA; 106223 MW; CB4ADE58CFAA8CD3 CRC64;
MQGKGLVKFA AIALTIACLY SLSFTWIANK VEKDAQEFAK GDAVKEKVYL DSVASLPVYS
SLSYITYQYA KEREIPLGLD LKGGMNVTME IALSDMVRNL ANNSTDANFN AAIKNAEVAM
ATGESDFIGV FGKEFEKISP NSKLSPLFAT KENSANLKID ASNEDVLNFL RKSADGAIDL
SFNILRTRID KFGVTSPNIQ KQQGTNRILI ELPGVTDPDR VRKLLQGSAK LEFWETYDNA
EIFSLLQNVN SILASTIKST DTSSASVAQD TTKSKLAALG KKDSSAVDSA AALSKVQAEQ
AKQNPLFALL NPATYQGQDG QVNLRPGPVV GYAALKDTAK VNSYLSSAAV RAVIPQNIRL
FWGVKPMSEE SKVFELYALK TSNLGGGPAL EGDVISDARS DYDQKGNPEV VMVMNADGAR
AWRSITAAAS ADPNNKKSVA IVLDNLVYSA PTVQGEIPNG ISSISGSFKV EDTQDLANVL
KAGRLPAPAK IVSDYVVGPS LGAASISAGL ISTIAGVIFI LLFMAMYYST AGLVANIALL
VNLFFLMGVL ASLGAVLTLP GIAGIVLSLG MSVDANVLIY ERIREELAEG KSARLAITEG
FKKAMPSILD SNITTFLTGV ILYIFGQGPI VGFATTLMIG IITSLFAAIF ISRLVFEWLL
DRKKPISFSI KATQNLFKDS KFDFITGRKR FYILSSAIIV AGIISAFTQG FSLGVDFQGG
RAYFVAFDKP VEVENVRSVL IDEFGTAVEV KTFGSSNQVK ITTAYLINDN SDQANDQVSS
KLASGLKKIN PVYEIKDSQK VTPTIAEDIK TSAIYATIFS ILVIFLYILA RFKRMAFGFA
AILALVHDVL VLLAIFTIFN GWLPFSLDID QAFIAAILTV MGYSINDTVV VFDRVREYIG
QHHSKNEDLP SVINNALNST LSRTVITGIC TIAVLLIIFI FGGEILRGFS FAMLIGVIFG
TYSSLFVATP FVVEFIKEKD KAKA
//
