YGIS_ECOLI
ID YGIS_ECOLI Reviewed; 535 AA.
AC Q46863; Q2M9I0;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Probable deoxycholate-binding periplasmic protein YgiS;
DE Flags: Precursor;
GN Name=ygiS; OrderedLocusNames=b3020, JW2988;
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 IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113;
RX PubMed=25534751; DOI=10.1111/1462-2920.12749;
RA Kwan B.W., Lord D.M., Peti W., Page R., Benedik M.J., Wood T.K.;
RT "The MqsR/MqsA toxin/antitoxin system protects Escherichia coli during bile
RT acid stress.";
RL Environ. Microbiol. 17:3168-3181(2015).
CC -!- FUNCTION: Probably part of a deoxycholate transport system. Its
CC expression in the presence of deoxycholate in a ygiS deletion mutant
CC increases intracellular deoxycholate levels and decreases cell growth;
CC higher expression in the presence of deoxycholate inhibits cell growth
CC completely. Bile acid detergents such as deoxycholate are important for
CC host defense against bacterial growth in the gall bladder and duodenum.
CC {ECO:0000269|PubMed:25534751}.
CC -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305|PubMed:25534751}.
CC -!- INDUCTION: Repressed by the toxin-antitoxin system MqsR-MqsA; this mRNA
CC is degraded by mRNA interferase MqsR. {ECO:0000269|PubMed:25534751}.
CC -!- DISRUPTION PHENOTYPE: Cells grow better in the presence of the bile
CC acid deoxycholate. Increased membrane stability when incubated for 2
CC hours in the presence of 4.5% deoxycholate. Increased cell survival in
CC the presence of 20% deoxycholate. {ECO:0000269|PubMed:25534751}.
CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 5 family.
CC {ECO:0000305}.
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DR EMBL; U28377; AAA69188.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76056.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77076.1; -; Genomic_DNA.
DR PIR; B65089; B65089.
DR RefSeq; NP_417492.1; NC_000913.3.
DR RefSeq; WP_001295629.1; NZ_SSZK01000023.1.
DR AlphaFoldDB; Q46863; -.
DR SMR; Q46863; -.
DR BioGRID; 4259246; 6.
DR STRING; 511145.b3020; -.
DR TCDB; 3.A.1.5.41; the atp-binding cassette (abc) superfamily.
DR jPOST; Q46863; -.
DR PaxDb; Q46863; -.
DR PRIDE; Q46863; -.
DR EnsemblBacteria; AAC76056; AAC76056; b3020.
DR EnsemblBacteria; BAE77076; BAE77076; BAE77076.
DR GeneID; 947140; -.
DR KEGG; ecj:JW2988; -.
DR KEGG; eco:b3020; -.
DR PATRIC; fig|1411691.4.peg.3710; -.
DR EchoBASE; EB2839; -.
DR eggNOG; COG4166; Bacteria.
DR HOGENOM; CLU_017028_0_3_6; -.
DR InParanoid; Q46863; -.
DR OMA; TMLDTMH; -.
DR PhylomeDB; Q46863; -.
DR BioCyc; EcoCyc:YGIS-MON; -.
DR PRO; PR:Q46863; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IDA:EcoCyc.
DR GO; GO:1904680; F:peptide transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015721; P:bile acid and bile salt transport; IDA:EcoCyc.
DR GO; GO:0015833; P:peptide transport; IBA:GO_Central.
DR InterPro; IPR030678; Peptide/Ni-bd.
DR InterPro; IPR039424; SBP_5.
DR InterPro; IPR000914; SBP_5_dom.
DR PANTHER; PTHR30290; PTHR30290; 1.
DR Pfam; PF00496; SBP_bac_5; 1.
DR PIRSF; PIRSF002741; MppA; 1.
PE 1: Evidence at protein level;
KW Periplasm; Reference proteome; Signal; Transport.
FT SIGNAL 1..20
FT /evidence="ECO:0000255"
FT CHAIN 21..535
FT /note="Probable deoxycholate-binding periplasmic protein
FT YgiS"
FT /id="PRO_0000031806"
SQ SEQUENCE 535 AA; 60694 MW; B0F56723071A54EF CRC64;
MYTRNLLWLV SLVSAAPLYA ADVPANTPLA PQQVFRYNNH SDPGTLDPQK VEENTAAQIV
LDLFEGLVWM DGEGQVQPAQ AERWEILDGG KRYIFHLRSG LQWSDGQPLT AEDFVLGWQR
AVDPKTASPF AGYLAQAHIN NAAAIVAGKA DVTSLGVKAT DDRTLEVTLE QPVPWFTTML
AWPTLFPVPH HVIAKHGDSW SKPENMVYNG AFVLDQWVVN EKITARKNPK YRDAQHTVLQ
QVEYLALDNS VTGYNRYRAG EVDLTWVPAQ QIPAIEKSLP GELRIIPRLN SEYYNFNLEK
PPFNDVRVRR ALYLTVDRQL IAQKVLGLRT PATTLTPPEV KGFSATTFDE LQKPMSERVA
MAKALLKQAG YDASHPLRFE LFYNKYDLHE KTAIALSSEW KKWLGAQVTL RTMEWKTYLD
ARRAGDFMLS RQSWDATYND ASSFLNTLKS DSEENVGHWK NAQYDALLNQ ATQITDATKR
NALYQQAEVI INQQAPLIPI YYQPLIKLLK PYVGGFPLHN PQDYVYSKEL YIKAH
