OPGG_ECOLI
ID OPGG_ECOLI Reviewed; 511 AA.
AC P33136;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1993, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Glucans biosynthesis protein G;
DE Flags: Precursor;
GN Name=mdoG; Synonyms=opgG; OrderedLocusNames=b1048, JW1035;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=7934824; DOI=10.1111/j.1365-2958.1993.tb01959.x;
RA Loubens I., Debarbieux L., Bohin A., Lacroix J.-M., Bohin J.-P.;
RT "Homology between a genetic locus (mdoA) involved in the osmoregulated
RT biosynthesis of periplasmic glucans in Escherichia coli and a genetic locus
RT (hrpM) controlling pathogenicity of Pseudomonas syringae.";
RL Mol. Microbiol. 10:329-340(1993).
RN [2]
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 [3]
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 [4]
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 [5]
RP PROTEIN SEQUENCE OF 23-34.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-511.
RX PubMed=15313617; DOI=10.1016/j.jmb.2004.07.004;
RA Hanoulle X., Rollet E., Clantin B., Landrieu I., Oedberg-Ferragut C.,
RA Lippens G., Bohin J.-P., Villeret V.;
RT "Structural analysis of Escherichia coli OpgG, a protein required for the
RT biosynthesis of osmoregulated periplasmic glucans.";
RL J. Mol. Biol. 342:195-205(2004).
CC -!- FUNCTION: Involved in the biosynthesis of osmoregulated periplasmic
CC glucans (OPGs).
CC -!- PATHWAY: Glycan metabolism; osmoregulated periplasmic glucan (OPG)
CC biosynthesis.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- DOMAIN: Contains a large N-terminal domain that would serve as the
CC catalytic core subunit, and a smaller C-terminal domain that would act
CC to modulate this enzymatic activity.
CC -!- SIMILARITY: Belongs to the OpgD/OpgG family. {ECO:0000305}.
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DR EMBL; X64197; CAA45521.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74132.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35846.1; -; Genomic_DNA.
DR PIR; S35417; S35417.
DR RefSeq; NP_415566.1; NC_000913.3.
DR RefSeq; WP_001343212.1; NZ_SSZK01000058.1.
DR PDB; 1TXK; X-ray; 2.50 A; A/B=23-511.
DR PDBsum; 1TXK; -.
DR AlphaFoldDB; P33136; -.
DR SMR; P33136; -.
DR BioGRID; 4260686; 331.
DR DIP; DIP-10177N; -.
DR IntAct; P33136; 6.
DR STRING; 511145.b1048; -.
DR SWISS-2DPAGE; P33136; -.
DR jPOST; P33136; -.
DR PaxDb; P33136; -.
DR PRIDE; P33136; -.
DR EnsemblBacteria; AAC74132; AAC74132; b1048.
DR EnsemblBacteria; BAA35846; BAA35846; BAA35846.
DR GeneID; 58463459; -.
DR GeneID; 945005; -.
DR KEGG; ecj:JW1035; -.
DR KEGG; eco:b1048; -.
DR PATRIC; fig|511145.12.peg.1090; -.
DR EchoBASE; EB1831; -.
DR eggNOG; COG3131; Bacteria.
DR HOGENOM; CLU_023403_2_0_6; -.
DR InParanoid; P33136; -.
DR OMA; KRPSAWI; -.
DR PhylomeDB; P33136; -.
DR BioCyc; EcoCyc:EG11885-MON; -.
DR UniPathway; UPA00637; -.
DR EvolutionaryTrace; P33136; -.
DR PRO; PR:P33136; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0051274; P:beta-glucan biosynthetic process; IDA:EcoCyc.
DR Gene3D; 2.60.40.10; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR HAMAP; MF_01069; MdoG_OpgG; 1.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR014438; Glucan_biosyn_MdoG/MdoD.
DR InterPro; IPR007444; Glucan_biosyn_MdoG_C.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR023704; MdoG_OpgG.
DR PANTHER; PTHR30504; PTHR30504; 1.
DR Pfam; PF04349; MdoG; 1.
DR PIRSF; PIRSF006281; MdoG; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Periplasm; Reference proteome;
KW Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000269|PubMed:9298646"
FT CHAIN 23..511
FT /note="Glucans biosynthesis protein G"
FT /id="PRO_0000020221"
FT HELIX 25..36
FT /evidence="ECO:0007829|PDB:1TXK"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:1TXK"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:1TXK"
FT TURN 71..73
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 79..84
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 103..105
FT /evidence="ECO:0007829|PDB:1TXK"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1TXK"
FT TURN 122..124
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 146..153
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 156..159
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 169..172
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 187..194
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 203..211
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 214..223
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 225..240
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 245..252
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 276..280
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 286..290
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 298..306
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:1TXK"
FT HELIX 319..321
FT /evidence="ECO:0007829|PDB:1TXK"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:1TXK"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 334..341
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 345..352
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 363..370
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 378..389
FT /evidence="ECO:0007829|PDB:1TXK"
FT HELIX 391..394
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 399..410
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 423..432
FT /evidence="ECO:0007829|PDB:1TXK"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 446..451
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 455..465
FT /evidence="ECO:0007829|PDB:1TXK"
FT TURN 466..469
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 470..480
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 486..493
FT /evidence="ECO:0007829|PDB:1TXK"
FT STRAND 495..507
FT /evidence="ECO:0007829|PDB:1TXK"
SQ SEQUENCE 511 AA; 57912 MW; 0B53ECE270516C70 CRC64;
MMKMRWLSAA VMLTLYTSSS WAFSIDDVAK QAQSLAGKGY ETPKSNLPSV FRDMKYADYQ
QIQFNHDKAY WNNLKTPFKL EFYHQGMYFD TPVKINEVTA TAVKRIKYSP DYFTFGDVQH
DKDTVKDLGF AGFKVLYPIN SKDKNDEIVS MLGASYFRVI GAGQVYGLSA RGLAIDTALP
SGEEFPRFKE FWIERPKPTD KRLTIYALLD SPRATGAYKF VVMPGRDTVV DVQSKIYLRD
KVGKLGVAPL TSMFLFGPNQ PSPANNYRPE LHDSNGLSIH AGNGEWIWRP LNNPKHLAVS
SFSMENPQGF GLLQRGRDFS RFEDLDDRYD LRPSAWVTPK GEWGKGSVEL VEIPTNDETN
DNIVAYWTPD QLPEPGKEMN FKYTITFSRD EDKLHAPDNA WVQQTRRSTG DVKQSNLIRQ
PDGTIAFVVD FTGAEMKKLP EDTPVTAQTS IGDNGEIVES TVRYNPVTKG WRLVMRVKVK
DAKKTTEMRA ALVNADQTLS ETWSYQLPAN E
