OPGC_SHIDS
ID OPGC_SHIDS Reviewed; 385 AA.
AC Q32E75;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 72.
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=SDY_2303;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(2005).
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; CP000034; ABB62380.1; -; Genomic_DNA.
DR RefSeq; WP_001070377.1; NC_007606.1.
DR RefSeq; YP_403871.1; NC_007606.1.
DR AlphaFoldDB; Q32E75; -.
DR STRING; 300267.SDY_2303; -.
DR EnsemblBacteria; ABB62380; ABB62380; SDY_2303.
DR KEGG; sdy:SDY_2303; -.
DR PATRIC; fig|300267.13.peg.2780; -.
DR HOGENOM; CLU_036182_2_0_6; -.
DR OMA; YFSYMLY; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000002716; 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_1000064516"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 60..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 173..193
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 212..232
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 274..294
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 338..358
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
SQ SEQUENCE 385 AA; 44760 MW; 9EF55F93D48DD6A3 CRC64;
MNPVPAQREY FLDSIRAWLM LLGIPFHISL IYSSHTWHVN STEPSLWLTL FNDFIHSFRM
QVFFVISGYF SYMLFLRYPL KKWWKVRVER VGIPMLTAIP LLTLPQFIML QYVKGKTKSW
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