YHES_ECOLI
ID YHES_ECOLI Reviewed; 637 AA.
AC P63389; P45535; Q2M718;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Probable ATP-binding protein YheS;
GN Name=yheS; OrderedLocusNames=b3352, JW3315;
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 / 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 [2]
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 [3]
RP FAMILY, AND MUTAGENESIS OF GLU-175 AND GLU-456.
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 -!- FUNCTION: Genetic data indicate it may be involved in ribosome assembly
CC or function. {ECO:0000305|PubMed:30597160}.
CC -!- INTERACTION:
CC P63389; P0AFG3: sucA; NbExp=3; IntAct=EBI-561198, EBI-543523;
CC P63389; P0CE47: tufA; NbExp=3; IntAct=EBI-561198, EBI-301077;
CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC YheS subfamily. {ECO:0000303|PubMed:30597160}.
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DR EMBL; U18997; AAA58149.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76377.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77938.1; -; Genomic_DNA.
DR PIR; C65129; C65129.
DR RefSeq; NP_417811.1; NC_000913.3.
DR RefSeq; WP_000634798.1; NZ_SSZK01000008.1.
DR AlphaFoldDB; P63389; -.
DR SMR; P63389; -.
DR BioGRID; 4260997; 19.
DR BioGRID; 852167; 6.
DR DIP; DIP-48200N; -.
DR IntAct; P63389; 11.
DR STRING; 511145.b3352; -.
DR jPOST; P63389; -.
DR PaxDb; P63389; -.
DR PRIDE; P63389; -.
DR EnsemblBacteria; AAC76377; AAC76377; b3352.
DR EnsemblBacteria; BAE77938; BAE77938; BAE77938.
DR GeneID; 66672767; -.
DR GeneID; 947856; -.
DR KEGG; ecj:JW3315; -.
DR KEGG; eco:b3352; -.
DR PATRIC; fig|1411691.4.peg.3378; -.
DR EchoBASE; EB2740; -.
DR eggNOG; COG0488; Bacteria.
DR HOGENOM; CLU_000604_36_0_6; -.
DR InParanoid; P63389; -.
DR OMA; CTHIADI; -.
DR PhylomeDB; P63389; -.
DR BioCyc; EcoCyc:YHES-MON; -.
DR PRO; PR:P63389; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; ISM:EcoCyc.
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; IPR017871; ABC_transporter-like_CS.
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; PS00211; ABC_TRANSPORTER_1; 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..637
FT /note="Probable ATP-binding protein YheS"
FT /id="PRO_0000093187"
FT DOMAIN 2..246
FT /note="ABC transporter 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT DOMAIN 313..527
FT /note="ABC transporter 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT REGION 523..559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 527..559
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
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 345..352
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT MUTAGEN 175
FT /note="E->Q: Causes growth defect at 37 degrees Celsius, 7-
FT fold decrease in translation; when associated with Q-456
FT (called EQ2)."
FT /evidence="ECO:0000269|PubMed:30597160"
FT MUTAGEN 456
FT /note="E->Q: Causes growth defect at 37 degrees Celsius, 7-
FT fold decrease in translation; when associated with Q-175
FT (EQ2)."
FT /evidence="ECO:0000269|PubMed:30597160"
SQ SEQUENCE 637 AA; 71843 MW; 81BC859FC1105EC5 CRC64;
MIVFSSLQIR RGVRVLLDNA TATINPGQKV GLVGKNGCGK STLLALLKNE ISADGGSYTF
PGSWQLAWVN QETPALPQAA LEYVIDGDRE YRQLEAQLHD ANERNDGHAI ATIHGKLDAI
DAWSIRSRAA SLLHGLGFSN EQLERPVSDF SGGWRMRLNL AQALICRSDL LLLDEPTNHL
DLDAVIWLEK WLKSYQGTLI LISHDRDFLD PIVDKIIHIE QQSMFEYTGN YSSFEVQRAT
RLAQQQAMYE SQQERVAHLQ SYIDRFRAKA TKAKQAQSRI KMLERMELIA PAHVDNPFRF
SFRAPESLPN PLLKMEKVSA GYGDRIILDS IKLNLVPGSR IGLLGRNGAG KSTLIKLLAG
ELAPVSGEIG LAKGIKLGYF AQHQLEYLRA DESPIQHLAR LAPQELEQKL RDYLGGFGFQ
GDKVTEETRR FSGGEKARLV LALIVWQRPN LLLLDEPTNH LDLDMRQALT EALIEFEGAL
VVVSHDRHLL RSTTDDLYLV HDRKVEPFDG DLEDYQQWLS DVQKQENQTD EAPKENANSA
QARKDQKRRE AELRAQTQPL RKEIARLEKE MEKLNAQLAQ AEEKLGDSEL YDQSRKAELT
ACLQQQASAK SGLEECEMAW LEAQEQLEQM LLEGQSN
