YTEP_BACSU
ID YTEP_BACSU Reviewed; 321 AA.
AC C0SPB3; O30504; O34826; Q795R3;
DT 16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Polygalacturonan/rhamnogalacturonan transport system permease protein YteP {ECO:0000305};
GN Name=yteP; Synonyms=yteQ; OrderedLocusNames=BSU30135;
GN ORFNames=BSU30130/BSU30140;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=9387221; DOI=10.1099/00221287-143-11-3431;
RA Lapidus A., Galleron N., Sorokin A., Ehrlich S.D.;
RT "Sequencing and functional annotation of the Bacillus subtilis genes in the
RT 200 kb rrnB-dnaB region.";
RL Microbiology 143:3431-3441(1997).
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.
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 INDUCTION, AND FUNCTION.
RC STRAIN=168;
RX PubMed=17449691; DOI=10.1128/aem.00147-07;
RA Ochiai A., Itoh T., Kawamata A., Hashimoto W., Murata K.;
RT "Plant cell wall degradation by saprophytic Bacillus subtilis strains: gene
RT clusters responsible for rhamnogalacturonan depolymerization.";
RL Appl. Environ. Microbiol. 73:3803-3813(2007).
RN [5]
RP FUNCTION, AND SUBUNIT.
RX PubMed=29240795; DOI=10.1371/journal.pone.0189483;
RA Ferreira M.J., Mendes A.L., de Sa-Nogueira I.;
RT "The MsmX ATPase plays a crucial role in pectin mobilization by Bacillus
RT subtilis.";
RL PLoS ONE 12:e0189483-e0189483(2017).
CC -!- FUNCTION: Involved in pectin degradation (PubMed:29240795). Part of the
CC ABC transporter complex YtcQP-YteP involved in the uptake of
CC polygalacturonan and rhamnogalacturonan type I (PubMed:17449691,
CC PubMed:29240795). Responsible for the translocation of the substrate
CC across the membrane (Probable). {ECO:0000269|PubMed:17449691,
CC ECO:0000269|PubMed:29240795, ECO:0000305}.
CC -!- SUBUNIT: The complex is probably composed of two ATP-binding proteins
CC (MsmX), two transmembrane proteins (YtcP and YteP) and a solute-binding
CC protein (YtcQ). {ECO:0000269|PubMed:29240795}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00441}.
CC -!- INDUCTION: Up-regulated by growth on type I rhamnogalacturonan.
CC {ECO:0000269|PubMed:17449691}.
CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC00270.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAC00271.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF008220; AAC00270.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AF008220; AAC00271.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB14992.2; -; Genomic_DNA.
DR PIR; G69990; G69990.
DR RefSeq; NP_390892.2; NC_000964.3.
DR RefSeq; WP_003229209.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; C0SPB3; -.
DR SMR; C0SPB3; -.
DR STRING; 224308.BSU30135; -.
DR PaxDb; C0SPB3; -.
DR PRIDE; C0SPB3; -.
DR EnsemblBacteria; CAB14992; CAB14992; BSU_30135.
DR GeneID; 937271; -.
DR KEGG; bsu:BSU30135; -.
DR PATRIC; fig|224308.179.peg.3270; -.
DR eggNOG; COG4209; Bacteria.
DR InParanoid; C0SPB3; -.
DR OMA; IWREAGW; -.
DR PhylomeDB; C0SPB3; -.
DR BioCyc; BSUB:BSU30135-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:0008643; P:carbohydrate transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR CDD; cd06261; TM_PBP2; 1.
DR Gene3D; 1.10.3720.10; -; 1.
DR InterPro; IPR000515; MetI-like.
DR InterPro; IPR035906; MetI-like_sf.
DR Pfam; PF00528; BPD_transp_1; 1.
DR SUPFAM; SSF161098; SSF161098; 1.
DR PROSITE; PS50928; ABC_TM1; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..321
FT /note="Polygalacturonan/rhamnogalacturonan transport system
FT permease protein YteP"
FT /id="PRO_0000378075"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 123..143
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 1..144
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 321 AA; 36656 MW; 6730D676977A3924 CRC64;
MKTAEAQAPA VDAVIFKKEK RKRLLIKLIQ QKYLYLMILP GCIYFLLFKY VPMWGIVIAF
QDYQPFLGIL GSEWVGLKHF IRLFTEPTFF LLLKNTLVLF ALNLAIFFPV PILLALLLNE
VRIALFKKFV QTLIYIPHFM SWVIVVSLSF VLLTVDGGLI NELIVFFGGE KINFLLNEEW
FRPLYILQVI WREAGWSTII YLAAITAVDP QLYEAAKMDG AGRLRQMWHI TLPAIKSVIV
VLLILKIGDT LELGFEHVYL LLNATNREVA EIFDTYVYTA GLKQGQFSYS TAVGVFKAAV
GLILVMLANR LAKKFGEEGI Y
