ID S5VD17_STRC3 Unreviewed; 369 AA.
AC S5VD17;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN Name=secF {ECO:0000256|HAMAP-Rule:MF_01464,
GN ECO:0000313|EMBL:AGS68387.1};
GN ORFNames=B446_07815 {ECO:0000313|EMBL:AGS68387.1};
OS Streptomyces collinus (strain DSM 40733 / Tue 365).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1214242 {ECO:0000313|EMBL:AGS68387.1, ECO:0000313|Proteomes:UP000015423};
RN [1] {ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RA Ruckert C., Szczepanowski R., Goesmann A., Pross E.K., Musiol E.M.,
RA Blin K., Wohlleben W., Puhler A., Weber T., Kalinowski J.;
RT "The complete genome sequence of Streptomyces collinus Tu 365.";
RL Submitted (OCT-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGS68387.1, ECO:0000313|Proteomes:UP000015423}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40733 / Tue 365 {ECO:0000313|Proteomes:UP000015423};
RX PubMed=24140291; DOI=10.1016/j.jbiotec.2013.10.004;
RA Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Iftime D.,
RA Musiol E.M., Blin K., Wohlleben W., Puhler A., Kalinowski J., Weber T.;
RT "Complete genome sequence of the kirromycin producer Streptomyces collinus
RT Tu 365 consisting of a linear chromosome and two linear plasmids.";
RL J. Biotechnol. 168:739-740(2013).
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; CP006259; AGS68387.1; -; Genomic_DNA.
DR RefSeq; WP_020938867.1; NC_021985.1.
DR AlphaFoldDB; S5VD17; -.
DR STRING; 1214242.B446_07815; -.
DR KEGG; sci:B446_07815; -.
DR PATRIC; fig|1214242.5.peg.1619; -.
DR eggNOG; COG0341; Bacteria.
DR HOGENOM; CLU_050012_2_0_11; -.
DR Proteomes; UP000015423; 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:UP000015423};
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 26..44
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 141..158
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 165..188
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 194..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 251..270
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 276..300
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT DOMAIN 112..304
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 329..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 369 AA; 39257 MW; 62A0387A2315F54F CRC64;
MSKLGNLGAR LHRGEISYDF VGKRKIWYGV SILITITAIL GLAVRGLNMG IEFQGGAVFT
TPVKMSTSVA QAEVFAKDAS GHEAIVQKLG NGSLRIQIAG IDTGKSDQIK TKLAQDLKLN
PEKLAADLVG PSWGEQIANK AWEGLGIFMV LVVIYLAIAF EWRMAIAALV ALIHDITITT
GIYALVGFEV TPGTVIGLLT ILGYSLYDTV VVFDSLKEQT KDITKQTRFT YSDIANQSIN
GTLVRSINTT VVALLPVAGL LFIGGGFLGA GTLNDISLSL FVGLAAGAYS SIFIATPLVA
DLKEREPAMK ALRKRVLAKR AQAAVGEDLA DARGTAGDES DDNAPAVVGP RNQPVSRNRG
RGRTSGKRR
//
