OPGC_SHIFL
ID OPGC_SHIFL Reviewed; 385 AA.
AC P67560; Q83RU4; Q8FIS5;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-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=SF1043, S1117;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN42665.2; -; Genomic_DNA.
DR EMBL; AE014073; AAP16549.1; -; Genomic_DNA.
DR RefSeq; NP_706958.2; NC_004337.2.
DR RefSeq; WP_001070350.1; NZ_WPGW01000143.1.
DR AlphaFoldDB; P67560; -.
DR STRING; 198214.SF1043; -.
DR EnsemblBacteria; AAN42665; AAN42665; SF1043.
DR EnsemblBacteria; AAP16549; AAP16549; S1117.
DR GeneID; 1023988; -.
DR GeneID; 66670685; -.
DR KEGG; sfl:SF1043; -.
DR KEGG; sfx:S1117; -.
DR PATRIC; fig|198214.7.peg.1215; -.
DR HOGENOM; CLU_036182_2_0_6; -.
DR OMA; YFSYMLY; -.
DR OrthoDB; 1979131at2; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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_0000218056"
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; 44700 MW; D8459ADC7C1E653C CRC64;
MNPVPAQREY FLDSIRAWLM LLGIPFHISL IYSSHTWHVN SAEPSLWLTL 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
