ID B4V683_9ACTN Unreviewed; 359 AA.
AC B4V683;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN ORFNames=M444_07915 {ECO:0000313|EMBL:AKL65331.1}, SSAG_03261
GN {ECO:0000313|EMBL:EDX23470.1};
OS Streptomyces sp. Mg1.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=465541 {ECO:0000313|EMBL:EDX23470.1, ECO:0000313|Proteomes:UP000005764};
RN [1] {ECO:0000313|EMBL:EDX23470.1, ECO:0000313|Proteomes:UP000005764}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:EDX23470.1,
RC ECO:0000313|Proteomes:UP000005764};
RG The Broad Institute Genome Sequencing Platform;
RA Fischbach M., Ward D., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Mehta T., Alvarado L., Kodira C.D., Straight P.,
RA Clardy J., Hung D., Kolter R., Mekalanos J., Walker S., Walsh C.T.,
RA Lander E., Galagan J., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. Mg1.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKL65331.1, ECO:0000313|Proteomes:UP000035653}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL65331.1,
RC ECO:0000313|Proteomes:UP000035653};
RX PubMed=23908282;
RA Hoefler B.C., Konganti K., Straight P.D.;
RT "De Novo Assembly of the Streptomyces sp. Strain Mg1 Genome Using PacBio
RT Single-Molecule Sequencing.";
RL Genome Announc. 1:e00535-13(2013).
RN [3] {ECO:0000313|EMBL:AKL65331.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Mg1 {ECO:0000313|EMBL:AKL65331.1};
RA Hoefler B.C., Straight P.D.;
RL Submitted (JUN-2015) 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_01464}.
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 -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01464}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01464}.
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DR EMBL; CP011664; AKL65331.1; -; Genomic_DNA.
DR EMBL; DS570400; EDX23470.1; -; Genomic_DNA.
DR RefSeq; WP_008740475.1; NZ_DS570400.1.
DR AlphaFoldDB; B4V683; -.
DR STRING; 465541.M444_07915; -.
DR KEGG; strm:M444_07915; -.
DR PATRIC; fig|465541.12.peg.1786; -.
DR eggNOG; COG0341; Bacteria.
DR HOGENOM; CLU_050012_2_0_11; -.
DR OrthoDB; 9774769at2; -.
DR Proteomes; UP000005764; Unassembled WGS sequence.
DR Proteomes; UP000035653; Chromosome.
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; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR HAMAP; MF_01464_B; SecF_B; 1.
DR InterPro; IPR022813; SecD/SecF_arch_bac.
DR InterPro; IPR022645; SecD/SecF_bac.
DR InterPro; IPR022646; SecD/SecF_CS.
DR InterPro; IPR048634; SecD_SecF_C.
DR InterPro; IPR005665; SecF_bac.
DR NCBIfam; TIGR00916; 2A0604s01; 1.
DR NCBIfam; TIGR00966; transloc_SecF; 1.
DR PANTHER; PTHR30081:SF8; PROTEIN TRANSLOCASE SUBUNIT SECF; 1.
DR PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR Pfam; PF07549; Sec_GG; 1.
DR Pfam; PF02355; SecD_SecF; 1.
DR PRINTS; PR01755; SECFTRNLCASE.
DR SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01464};
KW Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW Rule:MF_01464}; Reference proteome {ECO:0000313|Proteomes:UP000035653};
KW Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01464};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01464}.
FT TRANSMEM 25..44
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 140..157
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 164..187
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 193..215
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 246..269
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 275..299
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT DOMAIN 111..303
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 322..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 359 AA; 37696 MW; 4F2DB874AE2299E4 CRC64;
MSKLGDLGAK LYRGEVGYDF VGKRFLWYGV SILITITAIV ALAVQGLNMG IEFKGGAVFT
TPKTAVSVAK ATEDAEKASG HDAIVQELGT GGLRIQITGL DTASAADVKK QLASDLKVDQ
AGINADLVGP SWGEQIANKA WTGLGVFMIL VVIYLAIAFE WRMAVAALIA LIHDLTITVG
VYALVGFEVT PGTVIGLLTI LGYSLYDTVV VFDGLKEGSK DITKQTRYTF SEIANRSING
TLVRSINTTV VALLPVGALL FIGGGFLGAG MLNDISLSLF VGLAAGAYSS IFIATPLVVD
LKEREPGMKA LKKRVLAKRE AAAARGESPE EGYGSDAEGD GEGGPQIVAQ PQGRAGRRR
//