EPSK_BACSU
ID EPSK_BACSU Reviewed; 505 AA.
AC P71060; C0H3R6; O08179; P71061; Q795I9; Q795J0; Q798P4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-JAN-2009, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Uncharacterized membrane protein EpsK;
GN Name=epsK; Synonyms=yvfA/yvfB; OrderedLocusNames=BSU34265;
GN ORFNames=BSU34270/BSU34260;
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;
RX PubMed=8969506; DOI=10.1099/13500872-142-11-3089;
RA Fabret C., Quentin Y., Chapal N., Guiseppi A., Haiech J., Denizot F.;
RT "Integrated mapping and sequencing of a 115 kb DNA fragment from Bacillus
RT subtilis: sequence analysis of a 21 kb segment containing the sigL locus.";
RL Microbiology 142:3089-3096(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Denizot F.;
RL Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP SEQUENCE REVISION.
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 [5]
RP PROBABLE FUNCTION, IDENTIFICATION OF FRAMESHIFT, AND INDUCTION.
RC STRAIN=168, and 3610;
RX PubMed=15661000; DOI=10.1111/j.1365-2958.2004.04440.x;
RA Kearns D.B., Chu F., Branda S.S., Kolter R., Losick R.;
RT "A master regulator for biofilm formation by Bacillus subtilis.";
RL Mol. Microbiol. 55:739-749(2005).
CC -!- FUNCTION: May be involved in the production of the exopolysaccharide
CC (EPS) component of the extracellular matrix during biofilm formation.
CC EPS is responsible for the adhesion of chains of cells into bundles.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- INDUCTION: Repressed by SinR. {ECO:0000269|PubMed:15661000}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA96478.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAA96479.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB07994.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAB07995.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; Z71928; CAA96478.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z71928; CAA96479.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z94043; CAB07994.1; ALT_FRAME; Genomic_DNA.
DR EMBL; Z94043; CAB07995.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAX52695.1; -; Genomic_DNA.
DR PIR; B70037; B70037.
DR PIR; C70037; C70037.
DR RefSeq; WP_010886617.1; NZ_JNCM01000033.1.
DR RefSeq; YP_003097789.1; NC_000964.3.
DR AlphaFoldDB; P71060; -.
DR SMR; P71060; -.
DR STRING; 224308.BSU34265; -.
DR EnsemblBacteria; CAX52695; CAX52695; BSU_34265.
DR GeneID; 8302980; -.
DR KEGG; bsu:BSU34265; -.
DR PATRIC; fig|224308.179.peg.3713; -.
DR eggNOG; COG2244; Bacteria.
DR InParanoid; P71060; -.
DR OMA; EAFGFVH; -.
DR BioCyc; BSUB:BSU34265-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR029303; Polysacc_synt_C.
DR InterPro; IPR002797; Polysacc_synth.
DR Pfam; PF01943; Polysacc_synt; 1.
DR Pfam; PF14667; Polysacc_synt_C; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Exopolysaccharide synthesis; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..505
FT /note="Uncharacterized membrane protein EpsK"
FT /id="PRO_0000360684"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 86..106
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 341..361
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 435..455
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 464..484
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 505 AA; 55055 MW; 7F2E2ED932D59A0A CRC64;
MKFTINFSAN LTAFLLSVFL SVWMTPFIVK TLGVEAFGFV HLTQNVINYF SVITVALSSV
VVRFFSVAAH RGEREKANAY ISNYLAASVL ISLLLLLPLA GSAFFIDRVM NVPQALLADV
RLSILIGSVL FILTFLMAGF GAAPFYANRL YITSSIQAVQ MLIRVLSVLL LFACFAPKIW
QIQLAALAGA VIASVLSFYF FKKLIPWFSF RMKDLSFRTS KELFQAGAWS SVNQIGVLLF
LQIDLLTANL MLGASASGKY AAIIQFPLLL RSLAGTVASL FAPIMTSYYS KGDMEGLMNY
ANKAVRLNGL LLALPAALLG GLAGPFLTIW LGPSFSTIAP LLFIHAGYLV VSLAFMPLFY
IWTAFNQQKT PAIVTLLLGA VNVVLAVTLS GPAHLGLYGI TLAGAISLIL KNAIFTPLYV
SRITGYKKHV FLKGIIGPLS AAVFAWTVCK AIQFIVKIDS WPSLIATGVT VSFCYAVFAF
MLVCTKEERQ LVLKRFRKTK GAVNL
