YBIT_ECOLI
ID YBIT_ECOLI Reviewed; 530 AA.
AC P0A9U3; P75790;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Probable ATP-binding protein YbiT;
GN Name=ybiT; OrderedLocusNames=b0820, JW0804;
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=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
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 FAMILY, AND MUTAGENESIS OF GLU-181 AND GLU-464.
RC STRAIN=K12 / BW25113;
RX PubMed=30597160; DOI=10.1016/j.jmb.2018.12.013;
RA Murina V., Kasari M., Takada H., Hinnu M., Saha C.K., Grimshaw J.W.,
RA Seki T., Reith M., Putrins M., Tenson T., Strahl H., Hauryliuk V.,
RA Atkinson G.C.;
RT "ABCF ATPases involved in protein synthesis, ribosome assembly and
RT antibiotic resistance: structural and functional diversification across the
RT tree of life.";
RL J. Mol. Biol. 431:3568-3590(2019).
CC -!- INTERACTION:
CC P0A9U3; P0AAH8: sapF; NbExp=2; IntAct=EBI-558999, EBI-558765;
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC YbiT subfamily. {ECO:0000303|PubMed:30597160}.
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DR EMBL; U00096; AAC73907.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35501.1; -; Genomic_DNA.
DR PIR; D64819; D64819.
DR RefSeq; NP_415341.1; NC_000913.3.
DR RefSeq; WP_000961458.1; NZ_STEB01000019.1.
DR AlphaFoldDB; P0A9U3; -.
DR SMR; P0A9U3; -.
DR BioGRID; 4260856; 21.
DR BioGRID; 849814; 1.
DR DIP; DIP-11439N; -.
DR IntAct; P0A9U3; 3.
DR STRING; 511145.b0820; -.
DR jPOST; P0A9U3; -.
DR PaxDb; P0A9U3; -.
DR PRIDE; P0A9U3; -.
DR EnsemblBacteria; AAC73907; AAC73907; b0820.
DR EnsemblBacteria; BAA35501; BAA35501; BAA35501.
DR GeneID; 66670907; -.
DR GeneID; 945440; -.
DR KEGG; ecj:JW0804; -.
DR KEGG; eco:b0820; -.
DR PATRIC; fig|1411691.4.peg.1458; -.
DR EchoBASE; EB3109; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR InParanoid; P0A9U3; -.
DR OMA; DWMGQWT; -.
DR PhylomeDB; P0A9U3; -.
DR BioCyc; EcoCyc:G6423-MON; -.
DR PRO; PR:P0A9U3; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IBA:GO_Central.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR032781; ABC_tran_Xtn.
DR InterPro; IPR003439; ABC_transporter-like_ATP-bd.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00005; ABC_tran; 2.
DR Pfam; PF12848; ABC_tran_Xtn; 1.
DR SMART; SM00382; AAA; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Nucleotide-binding; Reference proteome; Repeat.
FT CHAIN 1..530
FT /note="Probable ATP-binding protein YbiT"
FT /id="PRO_0000093158"
FT DOMAIN 2..252
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 320..526
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 34..41
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT BINDING 352..359
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 181
FT /note="E->Q: Causes growth defect at 37 degrees Celsius,
FT 15-fold decrease in translation; when associated with Q-464
FT (called EQ2)."
FT /evidence="ECO:0000269|PubMed:30597160"
FT MUTAGEN 464
FT /note="E->Q: Causes growth defect at 37 degrees Celsius,
FT 15-fold decrease in translation; when associated with Q-181
FT (EQ2)."
FT /evidence="ECO:0000269|PubMed:30597160"
SQ SEQUENCE 530 AA; 59858 MW; EE75D66B5A58729A CRC64;
MLVSSNVTMQ FGSKPLFENI SVKFGGGNRY GLIGANGSGK STFMKILGGD LEPTLGNVSL
DPNERIGKLR QDQFAFEEFT VLDTVIMGHK ELWEVKQERD RIYALPEMSE EDGYKVADLE
VKYGEMDGYS AEARAGELLL GVGIPVEQHY GPMSEVAPGW KLRVLLAQAL FADPDILLLD
EPTNNLDIDT IRWLEQVLNE RDSTMIIISH DRHFLNMVCT HMADLDYGEL RVYPGNYDEY
MTAATQARER LLADNAKKKA QIAELQSFVS RFSANASKSR QATSRARQID KIKLEEVKAS
SRQNPFIRFE QDKKLFRNAL EVEGLTKGFD NGPLFKNLNL LLEVGEKLAV LGTNGVGKST
LLKTLVGDLQ PDSGTVKWSE NARIGYYAQD HEYEFENDLT VFEWMSQWKQ EGDDEQAVRS
ILGRLLFSQD DIKKPAKVLS GGEKGRMLFG KLMMQKPNIL IMDEPTNHLD MESIESLNMA
LELYQGTLIF VSHDREFVSS LATRILEITP ERVIDFSGNY EDYLRSKGIE
