OPGC_ECO57
ID OPGC_ECO57 Reviewed; 385 AA.
AC Q8X9I6;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Glucans biosynthesis protein C {ECO:0000255|HAMAP-Rule:MF_01066};
DE EC=2.1.-.- {ECO:0000255|HAMAP-Rule:MF_01066};
GN Name=mdoC {ECO:0000255|HAMAP-Rule:MF_01066};
GN Synonyms=opgC {ECO:0000255|HAMAP-Rule:MF_01066};
GN OrderedLocusNames=Z1681, ECs1425;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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. {ECO:0000255|HAMAP-Rule:MF_01066}.
CC -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01066}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01066};
CC Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01066}.
CC -!- SIMILARITY: Belongs to the acyltransferase 3 family. OpgC subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01066}.
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DR EMBL; AE005174; AAG55793.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB34848.1; -; Genomic_DNA.
DR PIR; A99807; A99807.
DR PIR; E85666; E85666.
DR RefSeq; NP_309452.1; NC_002695.1.
DR RefSeq; WP_001070358.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; Q8X9I6; -.
DR STRING; 155864.EDL933_1622; -.
DR EnsemblBacteria; AAG55793; AAG55793; Z1681.
DR EnsemblBacteria; BAB34848; BAB34848; ECs_1425.
DR GeneID; 914215; -.
DR KEGG; ece:Z1681; -.
DR KEGG; ecs:ECs_1425; -.
DR PATRIC; fig|386585.9.peg.1526; -.
DR eggNOG; COG1835; Bacteria.
DR HOGENOM; CLU_036182_2_0_6; -.
DR OMA; YFSYMLY; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0016741; F:transferase activity, transferring one-carbon groups; IEA:UniProtKB-UniRule.
DR GO; GO:0009250; P:glucan biosynthetic process; IEA:UniProtKB-UniRule.
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 3: Inferred from homology;
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_0000218051"
FT TRANSMEM 17..39
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 54..76
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 88..110
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 136..158
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 179..198
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 213..235
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 242..261
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 276..295
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 308..330
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 334..356
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
SQ SEQUENCE 385 AA; 44670 MW; 22D8269023D686A1 CRC64;
MNPVPAQREY FLDSIRAWLM LLGIPFHISL IYSSHTWHVN SAEPSLWLTL FNDFIHSFRM
QVFFVISGYF SYMLFLRYPL KKWWKVRVER VGIPMLTAIP LLTLPQFIML QYVKGKAESW
PGLSLYDKYN TLAWELISHL WFLLVLVVMT TLCVWIFKRI RNNLENSDKT NKKFSMVKLS
VIFLCLGIGY AVIRRTIFIV YPPILSNGTF NFIVMQTLFY LPFFILGALA FIFPHLKALF
TTPSRGCTLA AALAFVAYLL NQRYGSGDAW MYETESVITM VLGLWMVNVV FSFGHRLLNF
QSARVTYFVN ASLFIYLVHH PLTLFFGAYI TPHITSNWLG FLCGLIFVVG IAIILYEIHL
RIPLLKFLFS GKPVVKREND KAPAR
