YTCP_BACSU
ID YTCP_BACSU Reviewed; 286 AA.
AC P53561; O34963;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Polygalacturonan/rhamnogalacturonan transport system permease protein YtcP {ECO:0000305};
GN Name=ytcP; OrderedLocusNames=BSU30170;
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=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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-253.
RX PubMed=8763940; DOI=10.1128/jb.178.14.4122-4130.1996;
RA Bower S., Perkins J.B., Yocum R.R., Howitt C.L., Rahaim P., Pero J.;
RT "Cloning, sequencing, and characterization of the Bacillus subtilis biotin
RT biosynthetic operon.";
RL J. Bacteriol. 178:4122-4130(1996).
RN [4]
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:29240795).
CC Responsible for the translocation of the substrate across the membrane
CC (Probable). {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 -!- SIMILARITY: Belongs to the binding-protein-dependent transport system
CC permease family. CysTW subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB17464.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF008220; AAC00268.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB14995.1; -; Genomic_DNA.
DR EMBL; U51868; AAB17464.1; ALT_INIT; Genomic_DNA.
DR PIR; G69989; G69989.
DR RefSeq; NP_390895.1; NC_000964.3.
DR RefSeq; WP_010886597.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; P53561; -.
DR SMR; P53561; -.
DR STRING; 224308.BSU30170; -.
DR PaxDb; P53561; -.
DR PRIDE; P53561; -.
DR EnsemblBacteria; CAB14995; CAB14995; BSU_30170.
DR GeneID; 938095; -.
DR KEGG; bsu:BSU30170; -.
DR PATRIC; fig|224308.43.peg.3156; -.
DR eggNOG; COG0395; Bacteria.
DR InParanoid; P53561; -.
DR OMA; MMWGNFF; -.
DR PhylomeDB; P53561; -.
DR BioCyc; BSUB:BSU30170-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..286
FT /note="Polygalacturonan/rhamnogalacturonan transport system
FT permease protein YtcP"
FT /id="PRO_0000060268"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 69..89
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 106..126
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 131..151
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
FT DOMAIN 69..271
FT /note="ABC transmembrane type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00441"
SQ SEQUENCE 286 AA; 31693 MW; 60E610731291C073 CRC64;
MKNRLFDMLI YGFLLMFALI CVLPFIHVIA ASFATVEEVV SKKFILIPTT FSLDAYRYIF
STDIIYKSLL VSVFVTVIGT AVSMFLSSLM AYGLSRRDLI GRQPLMFLVV FTMLFSGGMI
PTFLVVKSLG LLDSYWALIL PTAINAFNLI ILKNFFQNIP SSLEESAKID GCNDLGIFFK
IVLPLSLPAI ATISLFYAVT YWNTYMTAIL YLNDSAKWPI QVLLRQIVIV SSGMQGDMSE
MGSGSPPPEQ TIKMAVIVVA TIPVLLVYPF IQKHFAKGAL LGSVKG
