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OPGC_ECOLI
ID   OPGC_ECOLI              Reviewed;         385 AA.
AC   P75920;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=Glucans biosynthesis protein C;
DE            EC=2.1.-.-;
GN   Name=mdoC; Synonyms=opgC, ymdD; OrderedLocusNames=b1047, JW1034;
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 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA   Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA   Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA   Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA   Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA   Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA   Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 12.7-28.0 min region on the linkage map.";
RL   DNA Res. 3:137-155(1996).
RN   [2]
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   [3]
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   [4]
RP   CHARACTERIZATION.
RX   PubMed=10368134; DOI=10.1128/jb.181.12.3626-3631.1999;
RA   Lacroix J.-M., Lanfroy E., Cogez V., Lequette Y., Bohin A., Bohin J.-P.;
RT   "The mdoC gene of Escherichia coli encodes a membrane protein that is
RT   required for succinylation of osmoregulated periplasmic glucans.";
RL   J. Bacteriol. 181:3626-3631(1999).
CC   -!- FUNCTION: Necessary for the succinyl substitution of periplasmic
CC       glucans. Could catalyze the transfer of succinyl residues from the
CC       cytoplasmic side of the membrane to the nascent glucan backbones on the
CC       periplasmic side of the membrane.
CC   -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC       biosynthesis.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the acyltransferase 3 family. OpgC subfamily.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC74131.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA35837.1; -; Genomic_DNA.
DR   PIR; D64847; D64847.
DR   RefSeq; NP_415565.1; NC_000913.3.
DR   RefSeq; WP_001070375.1; NZ_SSZK01000058.1.
DR   AlphaFoldDB; P75920; -.
DR   BioGRID; 4260688; 280.
DR   STRING; 511145.b1047; -.
DR   TCDB; 9.B.97.7.1; the acyltransferase-3/putative acetyl-coa transporter (atat) family.
DR   PaxDb; P75920; -.
DR   PRIDE; P75920; -.
DR   EnsemblBacteria; AAC74131; AAC74131; b1047.
DR   EnsemblBacteria; BAA35837; BAA35837; BAA35837.
DR   GeneID; 946944; -.
DR   KEGG; ecj:JW1034; -.
DR   KEGG; eco:b1047; -.
DR   PATRIC; fig|1411691.4.peg.1222; -.
DR   EchoBASE; EB3635; -.
DR   eggNOG; COG1835; Bacteria.
DR   HOGENOM; CLU_036182_2_0_6; -.
DR   InParanoid; P75920; -.
DR   OMA; YFSYMLY; -.
DR   PhylomeDB; P75920; -.
DR   BioCyc; EcoCyc:G6552-MON; -.
DR   UniPathway; UPA00637; -.
DR   PRO; PR:P75920; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR   GO; GO:0005886; C:plasma membrane; ISM:EcoCyc.
DR   GO; GO:0016748; F:succinyltransferase activity; IMP:EcoCyc.
DR   GO; GO:0016741; F:transferase activity, transferring one-carbon groups; IEA:UniProtKB-UniRule.
DR   GO; GO:1900727; P:osmoregulated periplasmic glucan biosynthetic process; IMP:EcoCyc.
DR   HAMAP; MF_01066; MdoC_OpgC; 1.
DR   InterPro; IPR002656; Acyl_transf_3_dom.
DR   InterPro; IPR023723; Glucans_biosynth_C.
DR   Pfam; PF01757; Acyl_transf_3; 1.
PE   1: Evidence at protein level;
KW   Acyltransferase; Cell membrane; Membrane; Reference proteome; Transferase;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..385
FT                   /note="Glucans biosynthesis protein C"
FT                   /id="PRO_0000218049"
FT   TRANSMEM        17..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        91..111
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        137..157
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        213..233
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        311..331
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        338..358
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   385 AA;  44690 MW;  24B869CE8E0224DF CRC64;
     MNPVPAQREY FLDSIRAWLM LLGIPFHISL IYSSHTWHVN SAESSLWLTL FNDFIHSFRM
     QVFFVISGYF SYMLFLRYPL KKWWKVRVER VGIPMLTAIP LLTLPQFIML QYVKGKAESW
     PGLSLYDKYN TLAWELISHL WFLLVLVVMT TLCVWIFKRI RNNLENSDKT NKKFSMVKLS
     VIFLCLGIGY AVIRRTIFIV YPPILSNGMF NFIVMQTLFY LPFFILGALA FIFPHLKALF
     TTPSRGCTLA AALAFVAYLL NQRYGSGDAW MYETESVITM VLGLWMVNVV FSFGHRLLNF
     QSARVTYFVN ASLFIYLVHH PLTLFFGAYI TPHITSNWLG FLCGLIFVVG IAIILYEIHL
     RIPLLKFLFS GKPVVKREND KAPAR
 
 
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