SKFF_BACSU
ID SKFF_BACSU Reviewed; 447 AA.
AC O31428; Q7DL61;
DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Putative bacteriocin-SkfA transport system permease protein SkfF;
GN Name=skfF {ECO:0000303|PubMed:12817086}; Synonyms=ybdB;
GN OrderedLocusNames=BSU01960;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Haga K., Liu H., Yasumoto K., Takahashi H., Yoshikawa H.;
RT "Sequence analysis of the 70kb region between 17 and 23 degree of the
RT Bacillus subtilis chromosome.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION TO 205; 216; 396; 412 AND 447.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP POSSIBLE FUNCTION IN SKFA SYNTHESIS, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / PY79;
RX PubMed=12817086; DOI=10.1126/science.1086462;
RA Gonzalez-Pastor J.E., Hobbs E.C., Losick R.;
RT "Cannibalism by sporulating bacteria.";
RL Science 301:510-513(2003).
RN [5]
RP REPRESSION BY ABRB AND ABH.
RX PubMed=17720793; DOI=10.1128/jb.01081-07;
RA Strauch M.A., Bobay B.G., Cavanagh J., Yao F., Wilson A., Le Breton Y.;
RT "Abh and AbrB control of Bacillus subtilis antimicrobial gene expression.";
RL J. Bacteriol. 189:7720-7732(2007).
CC -!- FUNCTION: Probably part of the ABC transporter SkfEF involved in the
CC export of the bacteriocin SKF. Probably responsible for the
CC translocation of bacteriocin SkfA across the membrane.
CC {ECO:0000305|PubMed:12817086}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: By Spo0A (PubMed:12817086) and PhoP, during nutrient
CC starvation, especially phosphate starvation. Repressed by AbrB during
CC normal growth when nutrients are plentiful, in association with the
CC transcriptional repressor Abh. {ECO:0000269|PubMed:12817086,
CC ECO:0000269|PubMed:17720793}.
CC -!- DISRUPTION PHENOTYPE: When the skfA-skfB-skfC-skfE-skfF-skfG-skfH
CC operon is deleted, increased rate of spore formation; a double operon
CC deletion (sdpA-sdpC plus skfA-skfH) makes spores even faster
CC (PubMed:12817086). {ECO:0000269|PubMed:12817086}.
CC -!- MISCELLANEOUS: Accelerated cannibalism by skf- cells is seen on solid
CC media but not in liquid media. {ECO:0000269|PubMed:12817086}.
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DR EMBL; AB006424; BAA33093.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB11990.2; -; Genomic_DNA.
DR PIR; A69747; A69747.
DR RefSeq; NP_388078.2; NC_000964.3.
DR RefSeq; WP_010886391.1; NC_000964.3.
DR AlphaFoldDB; O31428; -.
DR STRING; 224308.BSU01960; -.
DR TCDB; 3.A.1.128.1; the atp-binding cassette (abc) superfamily.
DR PaxDb; O31428; -.
DR PRIDE; O31428; -.
DR EnsemblBacteria; CAB11990; CAB11990; BSU_01960.
DR GeneID; 938494; -.
DR KEGG; bsu:BSU01960; -.
DR PATRIC; fig|224308.43.peg.198; -.
DR eggNOG; ENOG503383K; Bacteria.
DR BioCyc; BSUB:BSU01960-MON; -.
DR Proteomes; UP000001570; 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:0030152; P:bacteriocin biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR030920; SkfF.
DR TIGRFAMs; TIGR04405; SkfF; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Bacteriocin biosynthesis; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..447
FT /note="Putative bacteriocin-SkfA transport system permease
FT protein SkfF"
FT /id="PRO_0000312741"
FT TOPO_DOM 1..3
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 4..22
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 23..29
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..59
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 81..85
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..104
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 105..113
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 135..141
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 142..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..189
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..208
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 209..247
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 269..297
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..341
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 342..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 361..363
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 364..382
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 383..404
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..426
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 427..447
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 205
FT /note="M -> I (in Ref. 1; BAA33093)"
FT /evidence="ECO:0000305"
FT CONFLICT 216
FT /note="M -> I (in Ref. 1; BAA33093)"
FT /evidence="ECO:0000305"
FT CONFLICT 396
FT /note="L -> LL (in Ref. 1; BAA33093)"
FT /evidence="ECO:0000305"
FT CONFLICT 412
FT /note="S -> T (in Ref. 1; BAA33093)"
FT /evidence="ECO:0000305"
FT CONFLICT 447
FT /note="R -> K (in Ref. 1; BAA33093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 447 AA; 51817 MW; 066BD5A67DAAA48B CRC64;
MPFLIMLLFV GAIGFQVSFV SRSTTWDMSI AGWVLTGVFI LYTAFGLFSN RLPSQMADII
WLYGTATSFS KVVYSVLFFS VTWKALLWII SAIFGDVLIV LLSGDHINLL GRSIIFVGLF
FIAEVWLMSV SCARTVKKMK RVYVLVFLLM LGIYSICLYR FFFLQHSSGI WESIARFISG
VGLVFDTLSP LYVVVFIGII TVSFMTIAFT SRQVEMKESL VKEAEFWEEF QERQFGSGQI
IQKPKTTWWG LQGLNGIWSF LWLELLLFKK YLFFHSIHTV MLSGVFYVVI FMYPEWFYLL
FFLIVSAVML SSYYSGIVRH SQSGTLHLFP GALWKKIIIL ELTNTVWLYI LYCVSITFMA
VGNLVYWYIY GLGIYIWFMT IRLFAFTHTN RNDIKLSLPQ YYKSFFMALG LSGICLYVIH
LLTADWYTLV VVVCIGSLSW CLFYRFR
