ID A0A286IKQ7_9BACT Unreviewed; 978 AA.
AC A0A286IKQ7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
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=SAMN06298216_1657 {ECO:0000313|EMBL:SOE21186.1};
OS Spirosomataceae bacterium TFI 002.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae.
OX NCBI_TaxID=1945892 {ECO:0000313|EMBL:SOE21186.1, ECO:0000313|Proteomes:UP000217493};
RN [1] {ECO:0000313|EMBL:SOE21186.1, ECO:0000313|Proteomes:UP000217493}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TFI 002 {ECO:0000313|EMBL:SOE21186.1,
RC ECO:0000313|Proteomes:UP000217493};
RA Ehlers B., Leendertz F.H.;
RL Submitted (SEP-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}.
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DR EMBL; LT907983; SOE21186.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A286IKQ7; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000217493; Chromosome i.
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:UP000217493};
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 485..505
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 510..532
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 538..557
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 578..602
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 608..633
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 667..685
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 789..809
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 816..838
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 850..871
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 904..922
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 928..952
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 182..238
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 466..636
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 764..955
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 978 AA; 106223 MW; E48538889FCCB8EF CRC64;
MRNKGGIIAL LVAFMAVSAY YLIRTYKANS IRKEASAFAM GADGNIDPVK KQRYLDSLWK
KPAFLGTTLE DLTKQELGLG LDLQGGMHVI LEVSQNEIVK ALASGSRDPR IDQALASASK
LAVTSSDNYV DLFNQEFKKI AADVPLARIF SNSSNRGELS PNSSDSDVIS YIKKEVDGAF
SRAFRIIQTR VDKFGVANPN LQTLPGTNRI QIELPGVDNP QRVRKLLSGT AKLEFCEVYE
QQEVGQSIDA FVGYLSSLDA GNKPAPAKAV TDSSSASDLA SQLTQSTGDS LSTDSLGNNL
FNRLFFINQG GFAVRTKDSS RVNEIMRRQA VKQLFPSNLT FHYDVKPFMN VNTNEEVVNL
YMVKDAGKAP LEGDVVTNAR QDYDPTNGRP DVSMQMNAVG ARKWQSLTAE NVGQRVAIML
DGYVYSAPNV NQEISGGNSS ISGDFSVEEA QDLANVLKAG KLPAPTNIIE EAVVGASVGQ
DAVRAGVISS LVGLLAVLVF VLLYYNQAGW IANVALIVNL LLLLGVMASF GATLTLPGIA
GMVLSVGMSV DANVLIYERV KEELNEGKTF AQAIKNGFRF AMPSIIDSNV TTLITGIILF
IFGTGLVLGF ATTLLIGIFT SLFCAIFVSR LIFDYYLKKG KTVKFFTDWS TKLFSDTKID
FIKNRKIFYM VSASIIIAGA ISIGIKGFGL GVDFKGGRTY VAKFEQTVNT EEVRKAMESS
LEGATAEVKT FGGFDQVKIT TAYKIENVAP EVEREIEAKI NAAVTSIEGN HGEVVSSSKV
GPTIANDTIW NSLKALVYSL ILTFIYIYIR FRSVAFSFGA VVAVFHDVLV ILGIFSIFNG
ILPFSLDVDQ AFVGAVLTLM GYSMNDTVVV FDRVREYLND KKRAKEDIET VINNALNSTL
SRTAVTGIAT LLVLLILLIF GGETIRGFIF AMFLGVIVGT YSSLYIAAPI VVDAMKRQLN
KERDAAQLEP AVAEAKKK
//
