ID   SECF_STRCO              Reviewed;         373 AA.
AC   Q53956;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Protein translocase subunit SecF;
GN   Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=SCO1515;
GN   ORFNames=SCL2.05c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A3(2) / NRRL B-16638;
RA   Loriaux A., Frare P., Brans A., Dusart J.;
RL   Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_01464}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01464};
CC       Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01464}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01464}.
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DR   EMBL; X85969; CAA59955.1; -; Genomic_DNA.
DR   EMBL; AL939109; CAB70917.1; -; Genomic_DNA.
DR   PIR; S52766; S52766.
DR   RefSeq; NP_625794.1; NC_003888.3.
DR   RefSeq; WP_003977312.1; NZ_VNID01000021.1.
DR   AlphaFoldDB; Q53956; -.
DR   SMR; Q53956; -.
DR   STRING; 100226.SCO1515; -.
DR   GeneID; 1096941; -.
DR   KEGG; sco:SCO1515; -.
DR   PATRIC; fig|100226.15.peg.1524; -.
DR   eggNOG; COG0341; Bacteria.
DR   HOGENOM; CLU_050012_2_0_11; -.
DR   InParanoid; Q53956; -.
DR   OMA; AFEWRMA; -.
DR   PhylomeDB; Q53956; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0015031; P:protein transport; IBA:GO_Central.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
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; IPR005665; SecF_bac.
DR   PANTHER; PTHR30081; PTHR30081; 1.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR00966; 3a0501s07; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Protein transport; Reference proteome;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..373
FT                   /note="Protein translocase subunit SecF"
FT                   /id="PRO_0000095987"
FT   TRANSMEM        26..46
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TRANSMEM        142..162
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TRANSMEM        193..213
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TRANSMEM        251..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TRANSMEM        280..300
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   REGION          322..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   373 AA;  39711 MW;  28C55B23C62F82ED CRC64;
     MSKLGTLGAR LHHGEVGYDF VKNRKIWYGI SILITITAIV GLAVRGLHMG IEFQGGAVFT
     TPKNMSASVA QTETWAEEAS GHDAIVQKLG DGSLRIQIAG TDTQQSDQIK EDLSKNLDVS
     AEKINADLVG PSWGDQIANK AWQGLGIFMV LVVIYLAIAF EWRMALAAFV ALIHDITITV
     GIYALVGFEV TPGTVIGLLT ILGYSLYDTV VVFDSLKEQT RDITKQTRWT YAEIANRSIN
     STLVRSINTT VVALLPVAGL LFIGGGVLGA GMLNDISLSL FVGLAAGAYS SIFIATPLVA
     DLKEAEPQMK ALKKRVLAKR AQGAAKGESA ESAADEGAYD ADEPDDAAPA VVGPRNQPAS
     RGRGRGRPSG KRR