OPGC_SALTY
ID OPGC_SALTY Reviewed; 384 AA.
AC Q8ZQ27;
DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 84.
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}; OrderedLocusNames=STM1149;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(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; AE006468; AAL20079.1; -; Genomic_DNA.
DR RefSeq; NP_460120.1; NC_003197.2.
DR RefSeq; WP_000100055.1; NC_003197.2.
DR AlphaFoldDB; Q8ZQ27; -.
DR STRING; 99287.STM1149; -.
DR PaxDb; Q8ZQ27; -.
DR EnsemblBacteria; AAL20079; AAL20079; STM1149.
DR GeneID; 1252667; -.
DR KEGG; stm:STM1149; -.
DR PATRIC; fig|99287.12.peg.1216; -.
DR HOGENOM; CLU_036182_2_0_6; -.
DR OMA; YFSYMLY; -.
DR PhylomeDB; Q8ZQ27; -.
DR BioCyc; SENT99287:STM1149-MON; -.
DR UniPathway; UPA00637; -.
DR Proteomes; UP000001014; 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..384
FT /note="Glucans biosynthesis protein C"
FT /id="PRO_0000218055"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01066"
FT TRANSMEM 54..74
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 140..160
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 240..260
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 384 AA; 44271 MW; 04CFDF7E929452E6 CRC64;
MSSVPAPREY FLDSIRAWLM LLGIPFHISL IYSTHSWHVN SAAPSWWLTL FNDFIHAFRM
QVFFVISGYF SYMLFLRYPL KHWWKVRVER VGIPMLTAIP LLTLPQFILL QYVKEKTENW
PTLSAYEKYN TLAWELISHL WFLLVLVILT TVSIGIFTWF QKRQETSKPR PAAISLAKLS
LIFFLLGVAY AAIRRIIFIV YPAILSDGMF NFIVMQTLFY VPFFILGALA FIHPDLKARF
TTPSRGCTLG AAVAFIAYLL NQRYGSGDAW MYETESVITM VMGLWMVNVV FSLGHRLLNF
QSARVTYFVN ASLFIYLVHH PLTLFFGAYI TPHISSNLIG FLCGLIFVMG IALILYEIHL
RIPLLKFLFS GKPPVKRESR ATIG