ID   YHES_ECOL6              Reviewed;         637 AA.
AC   A0A0H2VBH0;
DT   26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 34.
DE   RecName: Full=Probable ATP-binding protein YheS;
GN   Name=yheS; OrderedLocusNames=c4127;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
RN   [2]
RP   DISRUPTION PHENOTYPE, AND MUTAGENESIS OF GLU-175 AND GLU-456.
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
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 (Probable). Ectopic expression exacerbates the cold-
CC       sensitive growth phenotype of a bipA deletion (PubMed:30597160).
CC       {ECO:0000269|PubMed:30597160, ECO:0000305|PubMed:30597160}.
CC   -!- DISRUPTION PHENOTYPE: No visible growth or ribosome-associated
CC       phenotype. {ECO:0000269|PubMed:30597160}.
CC   -!- SIMILARITY: Belongs to the ABC transporter superfamily. ABCF family.
CC       YheS subfamily. {ECO:0000303|PubMed:30597160}.
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DR   EMBL; AE014075; AAN82565.1; -; Genomic_DNA.
DR   RefSeq; WP_000634808.1; NC_004431.1.
DR   AlphaFoldDB; A0A0H2VBH0; -.
DR   SMR; A0A0H2VBH0; -.
DR   STRING; 199310.c4127; -.
DR   EnsemblBacteria; AAN82565; AAN82565; c4127.
DR   KEGG; ecc:c4127; -.
DR   eggNOG; COG0488; Bacteria.
DR   HOGENOM; CLU_000604_36_0_6; -.
DR   OMA; CTHIADI; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; Repeat.
FT   CHAIN           1..637
FT                   /note="Probable ATP-binding protein YheS"
FT                   /id="PRO_0000449036"
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                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   BINDING         345..352
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00434"
FT   MUTAGEN         175
FT                   /note="E->Q: Causes growth defect at 18 degrees Celsius in
FT                   bipA deletion strain; when associated with Q-456 (called
FT                   EQ2)."
FT                   /evidence="ECO:0000269|PubMed:30597160"
FT   MUTAGEN         456
FT                   /note="E->Q: Causes growth defect at 18 degrees Celsius in
FT                   bipA deletion strain; when associated with Q-175 (EQ2)."
FT                   /evidence="ECO:0000269|PubMed:30597160"
SQ   SEQUENCE   637 AA;  71870 MW;  21BC842F268E3F73 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 DESPLQHLAR LAPQELEQKL RDYLGGFGFQ
     GDKVTEETRR FSGGEKARLV LALIVWQRPN LLLLDEPTNH LDLDMRQALT EALIEFEGAL
     VVVSHDRHLL RSTTDDLYLV HDRKVEPFDG DLEDYQQWLS DVQKQENQTD EAPKENANSA
     QARKDQKRRE AELRAQTQPL RKEIARLEKE MEKLNAQLAQ AEEKLGDSEL YDQNRKAELT
     ACLQQQASAK SGLEECEMAW LEAQEQLEQM LLEGQSN