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CNTI_PSEAB
ID   CNTI_PSEAB              Reviewed;         284 AA.
AC   A0A0H2ZHZ4;
DT   05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 22.
DE   RecName: Full=Pseudopaline exporter CntI {ECO:0000305};
GN   Name=cntI {ECO:0000303|PubMed:29214991};
GN   Synonyms=zrmD {ECO:0000303|PubMed:28898501};
GN   OrderedLocusNames=PA14_63910 {ECO:0000312|EMBL:ABJ14218.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14;
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA   Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
RN   [2]
RP   INDUCTION.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=28898501; DOI=10.1111/mmi.13834;
RA   Mastropasqua M.C., D'Orazio M., Cerasi M., Pacello F., Gismondi A.,
RA   Canini A., Canuti L., Consalvo A., Ciavardelli D., Chirullo B.,
RA   Pasquali P., Battistoni A.;
RT   "Growth of Pseudomonas aeruginosa in zinc poor environments is promoted by
RT   a nicotianamine-related metallophore.";
RL   Mol. Microbiol. 106:543-561(2017).
RN   [3]
RP   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=UCBPP-PA14;
RX   PubMed=29214991; DOI=10.1038/s41598-017-16765-9;
RA   Lhospice S., Gomez N.O., Ouerdane L., Brutesco C., Ghssein G., Hajjar C.,
RA   Liratni A., Wang S., Richaud P., Bleves S., Ball G., Borezee-Durant E.,
RA   Lobinski R., Pignol D., Arnoux P., Voulhoux R.;
RT   "Pseudomonas aeruginosa zinc uptake in chelating environment is primarily
RT   mediated by the metallophore pseudopaline.";
RL   Sci. Rep. 7:17132-17132(2017).
CC   -!- FUNCTION: Transports the metallophore pseudopaline, which is involved
CC       in the acquisition of nickel and zinc, and thus enables bacterial
CC       growth inside the host, where metal access is limited. Is probably
CC       involved in the export of pseudopaline. {ECO:0000269|PubMed:29214991}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000305|PubMed:29214991}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- INDUCTION: Is part of the operon cntOLMI that is negatively regulated
CC       by zinc level through the Zur repressor, which leads to transcriptional
CC       activation of this operon under zinc depletion.
CC       {ECO:0000269|PubMed:28898501, ECO:0000269|PubMed:29214991}.
CC   -!- DISRUPTION PHENOTYPE: Mutant shows a large decrease in the
CC       extracellular pseudopaline level, with a concomitant increase in the
CC       intracellular space. Mutant is unable to grow in airway mucus
CC       secretions (AMS) and is impaired in iron accumulation in this media
CC       supplemented with iron. {ECO:0000269|PubMed:29214991}.
CC   -!- SIMILARITY: Belongs to the EamA transporter family. {ECO:0000305}.
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DR   EMBL; CP000438; ABJ14218.1; -; Genomic_DNA.
DR   RefSeq; WP_004365418.1; NZ_CP034244.1.
DR   AlphaFoldDB; A0A0H2ZHZ4; -.
DR   SMR; A0A0H2ZHZ4; -.
DR   EnsemblBacteria; ABJ14218; ABJ14218; PA14_63910.
DR   KEGG; pau:PA14_63910; -.
DR   HOGENOM; CLU_032828_0_1_6; -.
DR   OMA; YSYVQIV; -.
DR   BioCyc; PAER208963:G1G74-5404-MON; -.
DR   Proteomes; UP000000653; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   InterPro; IPR000620; EamA_dom.
DR   Pfam; PF00892; EamA; 2.
PE   2: Evidence at transcript level;
KW   Cell inner membrane; Cell membrane; Membrane; Repeat; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..284
FT                   /note="Pseudopaline exporter CntI"
FT                   /id="PRO_0000447265"
FT   TRANSMEM        2..22
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        74..94
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        96..116
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        122..142
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        147..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        259..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          8..138
FT                   /note="EamA 1"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          151..279
FT                   /note="EamA 2"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   284 AA;  30696 MW;  F8589AF42175CFE7 CRC64;
     MVLDLLKSGV LLAVLASFTF SVMNALVKEA SATLPAAEIV FFRSAIGTLL IYLLMRQAGV
     ALSRQGVPML LVRGVMGALY LVCYFYAIAH IPLADASILA HMSPFFVILF SALFLGERIP
     RAVYWLLLVV VLGALMIVKP FSYSSYSVYA VVGLLSAVFA AGASVAIRQL SARHHTYEIV
     FYFLAVATLV AIPLMWSDFV VPATLREWGL LLAIGVVSLL GQVFLTRAFS HESATIVAVT
     RYIGIVFNAG WGWLFWSEVP DALTIAGGVL IVVACIALSR TKKG
 
 
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