GABP_BACSU
ID GABP_BACSU Reviewed; 469 AA.
AC P46349; P94473;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 3.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Gamma-aminobutyric acid permease {ECO:0000303|PubMed:8951816};
DE Short=GABA permease {ECO:0000303|PubMed:8951816};
DE AltName: Full=4-aminobutyrate permease {ECO:0000303|PubMed:9677314};
DE AltName: Full=Gamma-aminobutyrate permease {ECO:0000303|PubMed:24142252};
DE AltName: Full=Proline transporter GabP {ECO:0000305};
GN Name=gabP {ECO:0000303|PubMed:8951816}; OrderedLocusNames=BSU06310;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=8951816; DOI=10.1046/j.1365-2958.1996.d01-1720.x;
RA Ferson A.E., Wray L.V. Jr., Fisher S.H.;
RT "Expression of the Bacillus subtilis gabP gene is regulated independently
RT in response to nitrogen and amino acid availability.";
RL Mol. Microbiol. 22:693-701(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969499; DOI=10.1099/13500872-142-11-3027;
RA Borriss R., Porwollik S., Schroeter R.;
RT "The 52 degrees-55 degrees segment of the Bacillus subtilis chromosome: a
RT region devoted to purine uptake and metabolism, and containing the genes
RT cotA, gabP and guaA and the pur gene cluster within a 34960 bp nucleotide
RT sequence.";
RL Microbiology 142:3027-3031(1996).
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 TO 36.
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 FUNCTION, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=9677314; DOI=10.1042/bj3330565;
RA Brechtel C.E., King S.C.;
RT "4-Aminobutyrate (GABA) transporters from the amine-polyamine-choline
RT superfamily: substrate specificity and ligand recognition profile of the 4-
RT aminobutyrate permease from Bacillus subtilis.";
RL Biochem. J. 333:565-571(1998).
RN [6]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION PHENOTYPE, AND
RP MUTAGENESIS OF GLY-33; GLY-42; GLY-301; GLY-338; PHE-341 AND GLY-414.
RC STRAIN=168 / JH642;
RX PubMed=24142252; DOI=10.1128/jb.01128-13;
RA Zaprasis A., Hoffmann T., Stannek L., Gunka K., Commichau F.M., Bremer E.;
RT "The gamma-aminobutyrate permease GabP serves as the third proline
RT transporter of Bacillus subtilis.";
RL J. Bacteriol. 196:515-526(2014).
CC -!- FUNCTION: Transporter for gamma-aminobutyrate (GABA) (PubMed:8951816,
CC PubMed:9677314, PubMed:24142252). Can also transport beta-alanine
CC (PubMed:9677314). Can translocate several open-chain GABA analogs (3-
CC aminobutyrate, 3-aminopropanoate, cis-4-aminobutenoate) across the
CC membrane via counterflow against GABA, but cannot transport muscimol
CC (PubMed:9677314). Functions also as a low-affinity proline importer
CC (PubMed:24142252). {ECO:0000269|PubMed:24142252,
CC ECO:0000269|PubMed:8951816, ECO:0000269|PubMed:9677314}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4-aminobutanoate(in) + H(+)(in) = 4-aminobutanoate(out) +
CC H(+)(out); Xref=Rhea:RHEA:28915, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:59888; Evidence={ECO:0000305|PubMed:8951816,
CC ECO:0000305|PubMed:9677314};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-alanine(in) + H(+)(in) = beta-alanine(out) + H(+)(out);
CC Xref=Rhea:RHEA:29459, ChEBI:CHEBI:15378, ChEBI:CHEBI:57966;
CC Evidence={ECO:0000305|PubMed:9677314};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=37 uM for GABA {ECO:0000269|PubMed:9677314};
CC KM=77 uM for GABA {ECO:0000269|PubMed:24142252};
CC KM=9.6 uM for beta-alanine {ECO:0000269|PubMed:9677314};
CC KM=1 mM for proline {ECO:0000269|PubMed:24142252};
CC Vmax=310 nmol/min/mg enzyme with GABA as substrate
CC {ECO:0000269|PubMed:24142252};
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC {ECO:0000269|PubMed:8951816}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: Positively regulated by TnrA under conditions of nitrogen
CC limitation (PubMed:8951816). Expression is not significantly induced by
CC GABA (PubMed:8951816). {ECO:0000269|PubMed:8951816}.
CC -!- DISRUPTION PHENOTYPE: A transposon insertion in this gene eliminates
CC the uptake of GABA and severely inhibits the utilization of GABA as a
CC nitrogen source (PubMed:8951816). Triple deletion of gabP, putP and
CC opuE confers resistance to the proline analog 3,4-dehydro-DL-proline
CC (DHP), abolishes GABA utilization and prevents use of proline as a
CC nitrogen source (PubMed:24142252). {ECO:0000269|PubMed:24142252,
CC ECO:0000269|PubMed:8951816}.
CC -!- MISCELLANEOUS: The ligand-recognition profile of the B.subtilis GabP
CC was found to differ substantially from that of the highly homologous
CC E.coli GabP. B.subtilis GabP exhibits more stringent requirements than
CC E.coli GabP for substrate recognition and translocation.
CC {ECO:0000269|PubMed:9677314}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Amino acid transporter (AAT) (TC 2.A.3.1) family.
CC {ECO:0000305}.
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DR EMBL; U31756; AAC44641.1; -; Genomic_DNA.
DR EMBL; U51115; AAB62306.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12450.2; -; Genomic_DNA.
DR PIR; C69628; C69628.
DR RefSeq; NP_388512.2; NC_000964.3.
DR RefSeq; WP_003233998.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; P46349; -.
DR SMR; P46349; -.
DR STRING; 224308.BSU06310; -.
DR TCDB; 2.A.3.1.5; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P46349; -.
DR PRIDE; P46349; -.
DR EnsemblBacteria; CAB12450; CAB12450; BSU_06310.
DR GeneID; 939485; -.
DR KEGG; bsu:BSU06310; -.
DR PATRIC; fig|224308.179.peg.684; -.
DR eggNOG; COG1113; Bacteria.
DR InParanoid; P46349; -.
DR OMA; TWNYCIQ; -.
DR PhylomeDB; P46349; -.
DR BioCyc; BSUB:BSU06310-MON; -.
DR SABIO-RK; P46349; -.
DR UniPathway; UPA00733; -.
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:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR InterPro; IPR004840; Amoino_acid_permease_CS.
DR InterPro; IPR011265; GABA_permease.
DR Pfam; PF00324; AA_permease; 1.
DR TIGRFAMs; TIGR01773; GABAperm; 1.
DR PROSITE; PS00218; AMINO_ACID_PERMEASE_1; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell membrane; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..469
FT /note="Gamma-aminobutyric acid permease"
FT /id="PRO_0000054201"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 18..38
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 61..94
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 95..115
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 116
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 117..137
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 138..157
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 179..200
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 201..221
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 222..242
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 243..263
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 264..269
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 270..290
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 291..328
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 350..355
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 356..376
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 377..401
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 423..425
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:24142252"
FT TRANSMEM 426..446
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 447..469
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:24142252"
FT MUTAGEN 33
FT /note="G->D: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24142252"
FT MUTAGEN 42
FT /note="G->S: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24142252"
FT MUTAGEN 301
FT /note="G->V: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24142252"
FT MUTAGEN 338
FT /note="G->E: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24142252"
FT MUTAGEN 341
FT /note="F->S: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24142252"
FT MUTAGEN 414
FT /note="G->R: Lack of activity."
FT /evidence="ECO:0000269|PubMed:24142252"
FT CONFLICT 36
FT /note="S -> P (in Ref. 2; AAB62306)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 469 AA; 51085 MW; 1F409F1B866F3A4D CRC64;
MNQSQSGLKK ELKTRHMTMI SIAGVIGAGL FVGSGSVIHS TGPGAVVSYA LAGLLVIFIM
RMLGEMSAVN PTSGSFSQYA HDAIGPWAGF TIGWLYWFFW VIVIAIEAIA GAGIIQYWFH
DIPLWLTSLI LTIVLTLTNV YSVKSFGEFE YWFSLIKVVT IIAFLIVGFA FIFGFAPGSE
PVGFSNLTGK GGFFPEGISS VLLGIVVVIF SFMGTEIVAI AAGETSNPIE SVTKATRSVV
WRIIVFYVGS IAIVVALLPW NSANILESPF VAVLEHIGVP AAAQIMNFIV LTAVLSCLNS
GLYTTSRMLY SLAERNEAPR RFMKLSKKGV PVQAIVAGTF FSYIAVVMNY FSPDTVFLFL
VNSSGAIALL VYLVIAVSQL KMRKKLEKTN PEALKIKMWL FPFLTYLTII AICGILVSMA
FIDSMRDELL LTGVITGIVL ISYLVFRKRK VSEKAAANPV TQQQPDILP
