ALLP_BACSU
ID ALLP_BACSU Reviewed; 490 AA.
AC P94575;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Allantoin permease {ECO:0000303|PubMed:11344136};
DE AltName: Full=Allantoin transport protein {ECO:0000303|PubMed:26967546};
DE AltName: Full=Allantoin transporter {ECO:0000303|PubMed:11344136};
GN Name=pucI {ECO:0000303|PubMed:11344136}; Synonyms=ywoE;
GN OrderedLocusNames=BSU36470;
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=9353933; DOI=10.1099/00221287-143-10-3313;
RA Presecan E., Moszer I., Boursier L., Cruz Ramos H., De La Fuente V.,
RA Hullo M.-F., Lelong C., Schleich S., Sekowska A., Song B.H., Villani G.,
RA Kunst F., Danchin A., Glaser P.;
RT "The Bacillus subtilis genome from gerBC (311 degrees) to licR (334
RT degrees).";
RL Microbiology 143:3313-3328(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 FUNCTION, AND INDUCTION.
RC STRAIN=168;
RX PubMed=11344136; DOI=10.1128/jb.183.11.3293-3302.2001;
RA Schultz A.C., Nygaard P., Saxild H.H.;
RT "Functional analysis of 14 genes that constitute the purine catabolic
RT pathway in Bacillus subtilis and evidence for a novel regulon controlled by
RT the PucR transcription activator.";
RL J. Bacteriol. 183:3293-3302(2001).
RN [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=26967546; DOI=10.1099/mic.0.000266;
RA Ma P., Patching S.G., Ivanova E., Baldwin J.M., Sharples D., Baldwin S.A.,
RA Henderson P.J.F.;
RT "Allantoin transport protein, PucI, from Bacillus subtilis: evolutionary
RT relationships, amplified expression, activity and specificity.";
RL Microbiology 162:823-836(2016).
CC -!- FUNCTION: Uptake of allantoin into the cell (PubMed:11344136,
CC PubMed:26967546). Allantoin uptake is not dependent on sodium, and PucI
CC is likely to be a proton-coupled symporter (PubMed:26967546). Shows
CC highest recognition for binding of allantoin, good recognition for
CC binding of hydantoin, L-5-benzylhydantoin and 5-hydroxyhydantoin, and
CC to a lesser extent for a range of nucleobases and nucleosides
CC (PubMed:26967546). {ECO:0000269|PubMed:11344136,
CC ECO:0000269|PubMed:26967546}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(S)-allantoin(in) + H(+)(in) = (S)-allantoin(out) + H(+)(out);
CC Xref=Rhea:RHEA:28723, ChEBI:CHEBI:15378, ChEBI:CHEBI:15678;
CC Evidence={ECO:0000305|PubMed:26967546};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28725;
CC Evidence={ECO:0000305|PubMed:26967546};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:26967546};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- INDUCTION: Expression is very low in excess nitrogen (glutamate plus
CC ammonia) and is induced during limiting-nitrogen conditions
CC (glutamate). Expression is further induced when allantoin or allantoate
CC are added during limiting-nitrogen conditions.
CC {ECO:0000269|PubMed:11344136}.
CC -!- SIMILARITY: Belongs to the purine-cytosine permease (2.A.39) family.
CC {ECO:0000305}.
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DR EMBL; Z82987; CAB05378.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15664.1; -; Genomic_DNA.
DR PIR; H70064; H70064.
DR RefSeq; NP_391528.1; NC_000964.3.
DR RefSeq; WP_003243156.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P94575; -.
DR SMR; P94575; -.
DR STRING; 224308.BSU36470; -.
DR TCDB; 2.A.39.3.4; the nucleobase:cation symporter-1 (ncs1) family.
DR PaxDb; P94575; -.
DR PRIDE; P94575; -.
DR EnsemblBacteria; CAB15664; CAB15664; BSU_36470.
DR GeneID; 936935; -.
DR KEGG; bsu:BSU36470; -.
DR PATRIC; fig|224308.179.peg.3946; -.
DR eggNOG; COG1953; Bacteria.
DR InParanoid; P94575; -.
DR OMA; GWNWRAV; -.
DR PhylomeDB; P94575; -.
DR BioCyc; BSUB:BSU36470-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:0015205; F:nucleobase transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015851; P:nucleobase transport; IBA:GO_Central.
DR InterPro; IPR012681; NCS1.
DR InterPro; IPR001248; Pur-cyt_permease.
DR InterPro; IPR045225; Uracil/uridine/allantoin_perm.
DR PANTHER; PTHR30618; PTHR30618; 1.
DR Pfam; PF02133; Transp_cyt_pur; 1.
DR TIGRFAMs; TIGR00800; ncs1; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Symport; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..490
FT /note="Allantoin permease"
FT /id="PRO_0000197931"
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 116..136
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 190..210
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 308..328
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 373..393
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 448..468
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 490 AA; 53982 MW; 2BB53F156B2294E6 CRC64;
MKLKESQQQS NRLSNEDLVP LGQEKRTWKA MNFASIWMGC IHNIPTYATV GGLIAIGLSP
WQVLAIIITA SLILFGALAL NGHAGTKYGL PFPVIIRASY GIYGANIPAL LRAFTAIMWL
GIQTFAGSTA LNILLLNMWP GWGEIGGEWN ILGIHLSGLL SFVFFWAIHL LVLHHGMESI
KRFEVWAGPL VYLVFGGMVW WAVDIAGGLG PIYSQPGKFH TFSETFWPFA AGVTGIIGIW
ATLILNIPDF TRFAETQKEQ IKGQFYGLPG TFALFAFASI TVTSGSQVAF GEPIWDVVDI
LARFDNPYVI VLSVITLCIA TISVNVAANI VSPAYDIANA LPKYINFKRG SFITALLALF
TVPWKLMESA TSVYAFLGLI GGMLGPVAGV MMADYFIIRK RELSVDDLYS ETGRYVYWKG
YNYRAFAATM LGALISLIGM YVPVLKSLYD ISWFVGVLIS FLFYIVLMRV HPPASLAIET
VEHAQVRQAE
