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OPUCC_LISM4
ID   OPUCC_LISM4             Reviewed;         308 AA.
AC   G2JZ42;
DT   11-JUL-2012, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2011, sequence version 1.
DT   25-MAY-2022, entry version 36.
DE   RecName: Full=Carnitine transport binding protein OpuCC;
DE   Flags: Precursor;
GN   Name=opuCC; OrderedLocusNames=LMRG_00878;
OS   Listeria monocytogenes serotype 1/2a (strain 10403S).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=393133;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10403S;
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Borowsky M., Borodovsky M., Young S.K., Zeng Q., Koehrsen M.,
RA   Fitzgerald M., Wiedmann M., Swaminathan B., Lauer P., Portnoy D.,
RA   Cossart P., Buchrieser C., Higgins D., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Borenstein D., Brown A., Chapman S.B., Chen Z.,
RA   Dunbar C.D., Engels R., Freedman E., Gearin G., Gellesch M., Goldberg J.,
RA   Griggs A., Gujja S., Heilman E., Heiman D., Howarth C., Jen D., Larson L.,
RA   Lui A., MacDonald J., Mehta T., Montmayeur A., Neiman D., Park D.,
RA   Pearson M., Priest M., Richards J., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Walk T., White J., Yandava C.,
RA   Haas B., Nusbaum C., Birren B.;
RT   "The genome sequence of Listeria monocytogenes strain 10403S.";
RL   Submitted (APR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   FUNCTION, INDUCTION, AND SUBUNIT.
RC   STRAIN=10403S;
RX   PubMed=12039715; DOI=10.1128/aem.68.6.2644-2650.2002;
RA   Angelidis A.S., Smith L.T., Hoffman L.M., Smith G.M.;
RT   "Identification of opuC as a chill-activated and osmotically activated
RT   carnitine transporter in Listeria monocytogenes.";
RL   Appl. Environ. Microbiol. 68:2644-2650(2002).
RN   [3]
RP   FUNCTION IN CARNITINE UPTAKE.
RC   STRAIN=10403S;
RX   PubMed=12406761; DOI=10.1128/aem.68.11.5647-5655.2002;
RA   Mendum M.L., Smith L.T.;
RT   "Gbu glycine betaine porter and carnitine uptake in osmotically stressed
RT   Listeria monocytogenes cells.";
RL   Appl. Environ. Microbiol. 68:5647-5655(2002).
RN   [4]
RP   FUNCTION IN CARNITINE AND GLYCINE BETAINE UPTAKE, AND INDUCTION.
RC   STRAIN=10403S;
RX   PubMed=12571024; DOI=10.1128/aem.69.2.1013-1022.2003;
RA   Angelidis A.S., Smith G.M.;
RT   "Three transporters mediate uptake of glycine betaine and carnitine by
RT   Listeria monocytogenes in response to hyperosmotic stress.";
RL   Appl. Environ. Microbiol. 69:1013-1022(2003).
RN   [5]
RP   INDUCTION.
RC   STRAIN=10403S;
RX   PubMed=12676677; DOI=10.1128/aem.69.4.2015-2022.2003;
RA   Fraser K.R., Sue D., Wiedmann M., Boor K., O'Byrne C.P.;
RT   "Role of sigmaB in regulating the compatible solute uptake systems of
RT   Listeria monocytogenes: osmotic induction of opuC is sigmaB dependent.";
RL   Appl. Environ. Microbiol. 69:2015-2022(2003).
CC   -!- FUNCTION: Part of the ABC transporter complex OpuCABCD involved in
CC       carnitine uptake. Involved, with BetL and GbuABC, in osmoprotection and
CC       cryoprotection of Listeria. Can also mediate weak glycine betaine
CC       transport. {ECO:0000269|PubMed:12039715, ECO:0000269|PubMed:12406761,
CC       ECO:0000269|PubMed:12571024}.
CC   -!- SUBUNIT: The complex is composed of two ATP-binding proteins (OpuCA),
CC       two transmembrane proteins (OpuCB and OpuCD) and a solute-binding
CC       protein (OpuCC). {ECO:0000305|PubMed:12039715}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE-ProRule:PRU00303}.
CC   -!- INDUCTION: The complex is induced by either hyperosmotic stress or by
CC       low temperature. Osmotic induction is sigma B-dependent.
CC       {ECO:0000269|PubMed:12039715, ECO:0000269|PubMed:12571024,
CC       ECO:0000269|PubMed:12676677}.
CC   -!- SIMILARITY: Belongs to the OsmX family. {ECO:0000305}.
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DR   EMBL; CP002002; AEO06411.1; -; Genomic_DNA.
DR   RefSeq; WP_003721931.1; NC_017544.1.
DR   AlphaFoldDB; G2JZ42; -.
DR   SMR; G2JZ42; -.
DR   EnsemblBacteria; AEO06411; AEO06411; LMRG_00878.
DR   KEGG; lmt:LMRG_00878; -.
DR   HOGENOM; CLU_038355_1_0_9; -.
DR   OMA; KDPAWKN; -.
DR   Proteomes; UP000001288; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR007210; ABC_Gly_betaine_transp_sub-bd.
DR   Pfam; PF04069; OpuAC; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Lipoprotein; Membrane; Palmitate; Signal; Stress response;
KW   Transport.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   CHAIN           23..308
FT                   /note="Carnitine transport binding protein OpuCC"
FT                   /id="PRO_0000418139"
FT   LIPID           23
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
FT   LIPID           23
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00303"
SQ   SEQUENCE   308 AA;  34549 MW;  79F8FEEA1CD97113 CRC64;
     MKKKFIALFS VLLLTSSLFL SSCSLPGLGG SSKDTIRIGA MATTESQIVS NILKELIEHD
     TGLKVEIVNN LGSTIVQHQA MLNGDVDITA TRYTGTDLVG PLGEEAIKDP EKALAAVKKG
     FEERFHQTWF DSYGFANTYV FMVRQDTAKK YNLNTVSDMR KVENELTAGV DNSWMEREGD
     GYKAFSKAYD IEFKKIFPMQ IGLIYTALKN NQMDVALGYS TDGRIPTYNL KLLKDDKKFF
     PPYDASALAT DEILKKHPEL KTTINKLKGK ISTEEMQKLN YEADGKLKEP SIVAQEFLQK
     NNYFEGKN
 
 
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