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ARGT_ECOLI
ID   ARGT_ECOLI              Reviewed;         260 AA.
AC   P09551; P77476;
DT   01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 3.
DT   03-AUG-2022, entry version 155.
DE   RecName: Full=Lysine/arginine/ornithine-binding periplasmic protein;
DE            Short=LAO-binding protein;
DE   Flags: Precursor;
GN   Name=argT; OrderedLocusNames=b2310, JW2307;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
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   [2]
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   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-146.
RC   STRAIN=K12;
RX   PubMed=3040734; DOI=10.1016/s0021-9258(18)45338-0;
RA   Nonet M.L., Marvel C.C., Tolan D.R.;
RT   "The hisT-purF region of the Escherichia coli K-12 chromosome.
RT   Identification of additional genes of the hisT and purF operons.";
RL   J. Biol. Chem. 262:12209-12217(1987).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-260.
RC   STRAIN=K12;
RA   Joshi A., Ames G.F.-L.;
RL   Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   PROTEIN SEQUENCE OF 23-34.
RC   STRAIN=K12 / EMG2;
RX   PubMed=9298646; DOI=10.1002/elps.1150180807;
RA   Link A.J., Robison K., Church G.M.;
RT   "Comparing the predicted and observed properties of proteins encoded in the
RT   genome of Escherichia coli K-12.";
RL   Electrophoresis 18:1259-1313(1997).
CC   -!- FUNCTION: Part of an ABC transporter involved in lysine, arginine and
CC       ornithine transport. Stimulates ATPase activity of HisP (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (HisP),
CC       two transmembrane proteins (HisM and HisQ) and a solute-binding protein
CC       (ArgT). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Periplasm.
CC   -!- SIMILARITY: Belongs to the bacterial solute-binding protein 3 family.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC75370.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA16156.1; -; Genomic_DNA.
DR   EMBL; M68935; AAA23971.1; -; Genomic_DNA.
DR   EMBL; U47027; AAA85768.1; -; Genomic_DNA.
DR   PIR; D65003; JKECT.
DR   RefSeq; NP_416813.1; NC_000913.3.
DR   RefSeq; WP_000748271.1; NZ_LN832404.1.
DR   AlphaFoldDB; P09551; -.
DR   SMR; P09551; -.
DR   BioGRID; 4260525; 19.
DR   ComplexPortal; CPX-4329; Polar amino acid ABC transporter complex.
DR   DIP; DIP-9148N; -.
DR   IntAct; P09551; 2.
DR   STRING; 511145.b2310; -.
DR   TCDB; 3.A.1.3.1; the atp-binding cassette (abc) superfamily.
DR   TCDB; 3.A.1.3.29; the atp-binding cassette (abc) superfamily.
DR   SWISS-2DPAGE; P09551; -.
DR   jPOST; P09551; -.
DR   PaxDb; P09551; -.
DR   PRIDE; P09551; -.
DR   EnsemblBacteria; AAC75370; AAC75370; b2310.
DR   EnsemblBacteria; BAA16156; BAA16156; BAA16156.
DR   GeneID; 58463739; -.
DR   GeneID; 949030; -.
DR   KEGG; ecj:JW2307; -.
DR   KEGG; eco:b2310; -.
DR   PATRIC; fig|1411691.4.peg.4424; -.
DR   EchoBASE; EB0070; -.
DR   eggNOG; COG0834; Bacteria.
DR   HOGENOM; CLU_019602_18_0_6; -.
DR   InParanoid; P09551; -.
DR   OMA; LYPTSYH; -.
DR   PhylomeDB; P09551; -.
DR   BioCyc; EcoCyc:ARGT-MON; -.
DR   PRO; PR:P09551; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0055052; C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing; IC:ComplexPortal.
DR   GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR   GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR   GO; GO:0089718; P:amino acid import across plasma membrane; IC:ComplexPortal.
DR   GO; GO:0006995; P:cellular response to nitrogen starvation; IEP:EcoCyc.
DR   GO; GO:0009267; P:cellular response to starvation; IEP:EcoCyc.
DR   GO; GO:0071294; P:cellular response to zinc ion; IEP:EcoCyc.
DR   GO; GO:1902022; P:L-lysine transport; ISO:EcoCyc.
DR   GO; GO:0015822; P:ornithine transport; ISO:EcoCyc.
DR   InterPro; IPR005768; Lys_Arg_Orn-bd.
DR   InterPro; IPR018313; SBP_3_CS.
DR   InterPro; IPR001638; Solute-binding_3/MltF_N.
DR   Pfam; PF00497; SBP_bac_3; 1.
DR   SMART; SM00062; PBPb; 1.
DR   TIGRFAMs; TIGR01096; 3A0103s03R; 1.
DR   PROSITE; PS01039; SBP_BACTERIAL_3; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Direct protein sequencing; Disulfide bond; Periplasm;
KW   Phosphoprotein; Reference proteome; Signal; Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000269|PubMed:9298646"
FT   CHAIN           23..260
FT                   /note="Lysine/arginine/ornithine-binding periplasmic
FT                   protein"
FT                   /id="PRO_0000031749"
FT   DISULFID        60..67
FT                   /evidence="ECO:0000250"
FT   CONFLICT        23
FT                   /note="A -> P (in Ref. 4; AAA23971)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        86..87
FT                   /note="ID -> ST (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        95
FT                   /note="I -> V (in Ref. 4)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        200..201
FT                   /note="FA -> SP (in Ref. 5; AAA85768)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        213
FT                   /note="F -> L (in Ref. 5; AAA85768)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        237..239
FT                   /note="GEL -> ACV (in Ref. 5; AAA85768)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   260 AA;  27992 MW;  E9BF1ECF0BB8A6FD CRC64;
     MKKSILALSL LVGLSTAASS YAALPETVRI GTDTTYAPFS SKDAKGDFVG FDIDLGNEMC
     KRMQVKCTWV ASDFDALIPS LKAKKIDAII SSLSITDKRQ QEIAFSDKLY AADSRLIAAK
     GSPIQPTLDS LKGKHVGVLQ GSTQEAYANE TWRSKGVDVV AYANQDLVYS DLAAGRLDAA
     LQDEVAASEG FLKQPAGKDF AFAGSSVKDK KYFGDGTGVG LRKDDAELTA AFNKALGELR
     QDGTYDKMAK KYFDFNVYGD
 
 
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