GABP_ECOLI
ID GABP_ECOLI Reviewed; 466 AA.
AC P25527;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Gamma-aminobutyric acid permease {ECO:0000303|PubMed:9806886};
DE Short=GABA permease {ECO:0000303|PubMed:8297211};
DE AltName: Full=4-aminobutyrate carrier {ECO:0000303|PubMed:8557687};
DE AltName: Full=4-aminobutyrate permease {ECO:0000305};
DE AltName: Full=Gamma-aminobutyrate permease {ECO:0000305};
GN Name=gabP {ECO:0000303|PubMed:8297211}; OrderedLocusNames=b2663, JW2638;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / JM103 / ATCC 39403 / DSM 2829 / KCTC 1112 / NCIMB 12044;
RX PubMed=8297211; DOI=10.1007/bf00245306;
RA Niegemann E., Schulz A., Bartsch K.;
RT "Molecular organization of the Escherichia coli gab cluster: nucleotide
RT sequence of the structural genes gabD and gabP and expression of the GABA
RT permease gene.";
RL Arch. Microbiol. 160:454-460(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / CS101B;
RA Metzer E., Halpern Y.S.;
RL Submitted (MAR-1992) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP PROTEIN SEQUENCE OF 2-11, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RX PubMed=11311234; DOI=10.1016/s0014-5793(01)02334-1;
RA Li X.D., Villa A., Gownley C., Kim M.J., Song J., Auer M., Wang D.N.;
RT "Monomeric state and ligand binding of recombinant GABA transporter from
RT Escherichia coli.";
RL FEBS Lett. 494:165-169(2001).
RN [7]
RP FUNCTION.
RX PubMed=8557687; DOI=10.1074/jbc.271.2.783;
RA Brechtel C.E., Hu L., King S.C.;
RT "Substrate specificity of the Escherichia coli 4-aminobutyrate carrier
RT encoded by gabP. Uptake and counterflow of structurally diverse
RT molecules.";
RL J. Biol. Chem. 271:783-788(1996).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY.
RX PubMed=9806886; DOI=10.1042/bj3360069;
RA Hu L.A., King S.C.;
RT "Membrane topology of the Escherichia coli gamma-aminobutyrate transporter:
RT implications on the topography and mechanism of prokaryotic and eukaryotic
RT transporters from the APC superfamily.";
RL Biochem. J. 336:69-76(1998).
RN [9]
RP INDUCTION.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=14731280; DOI=10.1046/j.1365-2958.2003.03867.x;
RA Metzner M., Germer J., Hengge R.;
RT "Multiple stress signal integration in the regulation of the complex sigma
RT S-dependent csiD-ygaF-gabDTP operon in Escherichia coli.";
RL Mol. Microbiol. 51:799-811(2004).
RN [10]
RP ACTIVITY REGULATION.
RX PubMed=15890647; DOI=10.1074/jbc.m504929200;
RA Zhang W., Campbell H.A., King S.C., Dowhan W.;
RT "Phospholipids as determinants of membrane protein topology.
RT Phosphatidylethanolamine is required for the proper topological
RT organization of the gamma-aminobutyric acid permease (GabP) of Escherichia
RT coli.";
RL J. Biol. Chem. 280:26032-26038(2005).
RN [11]
RP TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
CC -!- FUNCTION: Transporter for gamma-aminobutyrate (GABA) (PubMed:8297211,
CC PubMed:8557687). Transport is driven by the membrane potential
CC (PubMed:8297211). Can also transport a number of GABA analogs such as
CC nipecotic acid or muscimol (PubMed:8557687).
CC {ECO:0000269|PubMed:8297211, ECO:0000269|PubMed:8557687}.
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:0000269|PubMed:8297211};
CC -!- ACTIVITY REGULATION: Uptake is stimulated by ammonium sulfate and
CC abolished by 2,4-dinitrophenol (PubMed:8297211). Is affected both
CC topologically and kinetically by phospholipid composition of the
CC membrane (PubMed:15890647). In cells lacking phosphatidylethanolamine
CC (PE), the N-terminal hairpin is inverted relative to the membrane and
CC the rate of GABA transport is reduced by more than 99%
CC (PubMed:15890647). {ECO:0000269|PubMed:15890647,
CC ECO:0000269|PubMed:8297211}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=11.8 uM for GABA {ECO:0000269|PubMed:8297211};
CC Vmax=0.33 nmol/min/mg enzyme {ECO:0000269|PubMed:8297211};
CC -!- PATHWAY: Amino-acid degradation; 4-aminobutanoate degradation.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11311234}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:11311234,
CC ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:9806886}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:9806886}.
CC -!- INDUCTION: Induced by RpoS, but not in response to multiple stress
CC conditions. {ECO:0000269|PubMed:14731280}.
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; M88334; AAC36833.1; -; Genomic_DNA.
DR EMBL; X65104; CAA46229.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75710.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16526.1; -; Genomic_DNA.
DR PIR; H65045; H65045.
DR RefSeq; NP_417149.1; NC_000913.3.
DR RefSeq; WP_001295173.1; NZ_STEB01000042.1.
DR AlphaFoldDB; P25527; -.
DR SMR; P25527; -.
DR BioGRID; 4261470; 22.
DR DIP; DIP-9724N; -.
DR IntAct; P25527; 2.
DR STRING; 511145.b2663; -.
DR TCDB; 2.A.3.1.4; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P25527; -.
DR PRIDE; P25527; -.
DR EnsemblBacteria; AAC75710; AAC75710; b2663.
DR EnsemblBacteria; BAA16526; BAA16526; BAA16526.
DR GeneID; 66673467; -.
DR GeneID; 948049; -.
DR KEGG; ecj:JW2638; -.
DR KEGG; eco:b2663; -.
DR PATRIC; fig|1411691.4.peg.4078; -.
DR EchoBASE; EB1306; -.
DR eggNOG; COG1113; Bacteria.
DR HOGENOM; CLU_007946_9_3_6; -.
DR InParanoid; P25527; -.
DR OMA; WEGGVHL; -.
DR PhylomeDB; P25527; -.
DR BioCyc; EcoCyc:GABP-MON; -.
DR BioCyc; MetaCyc:GABP-MON; -.
DR UniPathway; UPA00733; -.
DR PRO; PR:P25527; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015185; F:gamma-aminobutyric acid transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015291; F:secondary active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:EcoCyc.
DR GO; GO:0009450; P:gamma-aminobutyric acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0015812; P:gamma-aminobutyric acid transport; IMP:EcoCyc.
DR GO; GO:0090549; P:response to carbon starvation; IEP:EcoCyc.
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 inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11311234"
FT CHAIN 2..466
FT /note="Gamma-aminobutyric acid permease"
FT /id="PRO_0000054202"
FT TOPO_DOM 2..20
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 63..96
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 118
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 119..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..199
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..246
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 268..286
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 287..307
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 308..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 356..358
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 380..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..428
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9806886"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..466
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:9806886"
FT CONFLICT 72
FT /note="T -> R (in Ref. 2; CAA46229)"
FT /evidence="ECO:0000305"
FT CONFLICT 385..386
FT /note="MR -> IG (in Ref. 2; CAA46229)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 466 AA; 51080 MW; 87998A83C80BA4EC CRC64;
MGQSSQPHEL GGGLKSRHVT MLSIAGVIGA SLFVGSSVAI AEAGPAVLLA YLFAGLLVVM
IMRMLAEMAV ATPDTGSFST YADKAIGRWA GYTIGWLYWW FWVLVIPLEA NIAAMILHSW
VPGIPIWLFS LVITLALTGS NLLSVKNYGE FEFWLALCKV IAILAFIFLG AVAISGFYPY
AEVSGISRLW DSGGFMPNGF GAVLSAMLIT MFSFMGAEIV TIAAAESDTP EKHIVRATNS
VIWRISIFYL CSIFVVVALI PWNMPGLKAV GSYRSVLELL NIPHAKLIMD CVILLSVTSC
LNSALYTASR MLYSLSRRGD APAVMGKINR SKTPYVAVLL STGAAFLTVV VNYYAPAKVF
KFLIDSSGAI ALLVYLVIAV SQLRMRKILR AEGSEIRLRM WLYPWLTWLV IGFITFVLVV
MLFRPAQQLE VISTGLLAIG IICTVPIMAR WKKLVLWQKT PVHNTR
