ABGT_ECOLI
ID ABGT_ECOLI Reviewed; 508 AA.
AC P46133; P76051; P76843; P76845;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 3.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=p-aminobenzoyl-glutamate transport protein;
DE AltName: Full=PABA-GLU transport protein;
GN Name=abgT; Synonyms=ydaH; OrderedLocusNames=b1336, JW5822;
GN ORFNames=ECK1332;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND INDUCTION.
RC STRAIN=BN1001, and BN1003;
RX PubMed=9829935; DOI=10.1128/jb.180.23.6260-6268.1998;
RA Hussein M.J., Green J.M., Nichols B.P.;
RT "Characterization of mutations that allow p-aminobenzoyl-glutamate
RT utilization by Escherichia coli.";
RL J. Bacteriol. 180:6260-6268(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 504.
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 [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 452-508.
RX PubMed=2825131; DOI=10.1093/nar/15.22.9177;
RA Potter P.M., Wilkinson M.C., Fitton J., Carr F.J., Brennand J.,
RA Cooper D.P., Margison G.P.;
RT "Characterisation and nucleotide sequence of ogt, the O6-alkylguanine-DNA-
RT alkyltransferase gene of E. coli.";
RL Nucleic Acids Res. 15:9177-9193(1987).
RN [6]
RP IDENTIFICATION.
RX PubMed=7567469; DOI=10.1093/nar/23.17.3554;
RA Borodovsky M., McIninch J., Koonin E.V., Rudd K.E., Medigue C., Danchin A.;
RT "Detection of new genes in a bacterial genome using Markov models for three
RT gene classes.";
RL Nucleic Acids Res. 23:3554-3562(1995).
RN [7]
RP 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).
RN [8]
RP FUNCTION AS A TRANSPORT PROTEIN, AND ACTIVITY REGULATION.
RX PubMed=17307853; DOI=10.1128/jb.01940-06;
RA Carter E.L., Jager L., Gardner L., Hall C.C., Willis S., Green J.M.;
RT "Escherichia coli abg genes enable uptake and cleavage of the folate
RT catabolite p-aminobenzoyl-glutamate.";
RL J. Bacteriol. 189:3329-3334(2007).
RN [9]
RP FUNCTION AS A TRANSPORT PROTEIN.
RX PubMed=20190044; DOI=10.1128/jb.01362-09;
RA Green J.M., Hollandsworth R., Pitstick L., Carter E.L.;
RT "Purification and characterization of the folate catabolic enzyme p-
RT aminobenzoyl-glutamate hydrolase from Escherichia coli.";
RL J. Bacteriol. 192:2407-2413(2010).
CC -!- FUNCTION: Essential for aminobenzoyl-glutamate utilization. It
CC catalyzes the concentration-dependent uptake of p-aminobenzoyl-
CC glutamate (PABA-GLU) into the cell and allows accumulation of PABA-GLU
CC to a concentration enabling AbgAB to catalyze cleavage into p-
CC aminobenzoate and glutamate. It seems also to increase the sensitivity
CC to low levels of aminobenzoyl-glutamate. May actually serve
CC physiologically as a transporter for some other molecule, perhaps a
CC dipeptide, and that it transports p-aminobenzoyl-glutamate as a
CC secondary activity. The physiological role of abgABT should be
CC clarified. {ECO:0000269|PubMed:17307853, ECO:0000269|PubMed:20190044}.
CC -!- ACTIVITY REGULATION: Completely inhibited by 100 nM of sodium azide and
CC slightly inhibited by 100 mM of potassium fluoride.
CC {ECO:0000269|PubMed:17307853}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996}.
CC -!- INDUCTION: Could be transcriptionally regulated by AbgR.
CC {ECO:0000269|PubMed:9829935}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene loss the p-aminobenzoyl-
CC glutamate utilization phenotype. {ECO:0000269|PubMed:9829935}.
CC -!- MISCELLANEOUS: It is suggested that in wild-type strain abgT would
CC normally be cryptic or not expressed under conditions of growth on
CC minimal medium. Altering the expression of abgT from its wild-type
CC context appears to be the mechanism for obtaining the growth phenotype
CC (PubMed:9829935). {ECO:0000305|PubMed:9829935}.
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DR EMBL; U00096; AAC74418.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA14929.2; -; Genomic_DNA.
DR EMBL; Y00495; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; C64883; C64883.
DR RefSeq; NP_415852.2; NC_000913.3.
DR RefSeq; WP_000062973.1; NZ_SSUW01000011.1.
DR AlphaFoldDB; P46133; -.
DR SMR; P46133; -.
DR BioGRID; 4260156; 187.
DR DIP; DIP-9031N; -.
DR IntAct; P46133; 1.
DR STRING; 511145.b1336; -.
DR TCDB; 2.A.68.1.1; the p-aminobenzoyl-glutamate transporter (abgt) family.
DR PaxDb; P46133; -.
DR PRIDE; P46133; -.
DR DNASU; 945912; -.
DR EnsemblBacteria; AAC74418; AAC74418; b1336.
DR EnsemblBacteria; BAA14929; BAA14929; BAA14929.
DR GeneID; 945912; -.
DR KEGG; ecj:JW5822; -.
DR KEGG; eco:b1336; -.
DR PATRIC; fig|1411691.4.peg.941; -.
DR EchoBASE; EB2697; -.
DR eggNOG; COG2978; Bacteria.
DR HOGENOM; CLU_040132_0_0_6; -.
DR InParanoid; P46133; -.
DR OMA; ELTQMAY; -.
DR PhylomeDB; P46133; -.
DR BioCyc; EcoCyc:ABGT-MON; -.
DR BioCyc; MetaCyc:ABGT-MON; -.
DR PRO; PR:P46133; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015558; F:secondary active p-aminobenzoyl-glutamate transmembrane transporter activity; IMP:EcoCyc.
DR GO; GO:0015291; F:secondary active transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:1902604; P:p-aminobenzoyl-glutamate transmembrane transport; IEA:InterPro.
DR GO; GO:0015814; P:p-aminobenzoyl-glutamate transport; IMP:EcoCyc.
DR InterPro; IPR004697; AbgT.
DR InterPro; IPR011540; AbgT_Proteobac.
DR PANTHER; PTHR30282; PTHR30282; 1.
DR Pfam; PF03806; ABG_transport; 1.
DR TIGRFAMs; TIGR00819; ydaH; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..508
FT /note="p-aminobenzoyl-glutamate transport protein"
FT /id="PRO_0000064422"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 85..105
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 121..139
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 140..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 164..184
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 405..425
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 479..499
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 504
FT /note="Y -> S (in Ref. 2; BAA14929)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 508 AA; 54886 MW; C33CBCBE7A39E951 CRC64;
MSMSSIPSSS QSGKLYGWVE RIGNKVPHPF LLFIYLIIVL MVTTAILSAF GVSAKNPTDG
TPVVVKNLLS VEGLHWFLPN VIKNFSGFAP LGAILALVLG AGLAERVGLL PALMVKMASH
VNARYASYMV LFIAFFSHIS SDAALVIMPP MGALIFLAVG RHPVAGLLAA IAGVGCGFTA
NLLIVTTDVL LSGISTEAAA AFNPQMHVSV IDNWYFMASS VVVLTIVGGL ITDKIIEPRL
GQWQGNSDEK LQTLTESQRF GLRIAGVVSL LFIAAIALMV IPQNGILRDP INHTVMPSPF
IKGIVPLIIL FFFVVSLAYG IATRTIRRQA DLPHLMIEPM KEMAGFIVMV FPLAQFVAMF
NWSNMGKFIA VGLTDILESS GLSGIPAFVG LALLSSFLCM FIASGSAIWS ILAPIFVPMF
MLLGFHPAFA QILFRIADSS VLPLAPVSPF VPLFLGFLQR YKPDAKLGTY YSLVLPYPLI
FLVVWLLMLL AWYLVGLPIG PGIYPRLS
