EGLC_RHIME
ID EGLC_RHIME Reviewed; 465 AA.
AC Q9Z3Q2;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 25-MAY-2022, entry version 126.
DE RecName: Full=Endo-1,3-1,4-beta-glycanase EglC;
DE EC=3.2.1.-;
DE AltName: Full=Succinoglycan biosynthesis protein EglC;
GN Name=eglC; OrderedLocusNames=RA0864; ORFNames=SMa1587;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymA (megaplasmid 1).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=CXM1-105;
RX PubMed=10485295; DOI=10.1007/s004380051052;
RA Sharypova L.A., Yurgel S.N., Keller M., Simarov B.V., Puehler A.,
RA Becker A.;
RT "The eff-482 locus of Sinorhizobium meliloti CXM1-105 that influences
RT symbiotic effectiveness consists of three genes encoding an endoglycanase,
RT a transcriptional regulator and an adenylate cyclase.";
RL Mol. Gen. Genet. 261:1032-1044(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481432; DOI=10.1073/pnas.161294798;
RA Barnett M.J., Fisher R.F., Jones T., Komp C., Abola A.P., Barloy-Hubler F.,
RA Bowser L., Capela D., Galibert F., Gouzy J., Gurjal M., Hong A., Huizar L.,
RA Hyman R.W., Kahn D., Kahn M.L., Kalman S., Keating D.H., Palm C.,
RA Peck M.C., Surzycki R., Wells D.H., Yeh K.-C., Davis R.W., Federspiel N.A.,
RA Long S.R.;
RT "Nucleotide sequence and predicted functions of the entire Sinorhizobium
RT meliloti pSymA megaplasmid.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9883-9888(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
CC -!- FUNCTION: Cleaves high molecular weight succinoglycan to yield LMW
CC succinoglycan. Dynamically regulates the molecular weight distribution
CC of succinoglycan by cleaving nascent succinoglycan only during a
CC limited period after its synthesis, perhaps before it undergoes a time-
CC dependent change in its conformation or aggregation state (By
CC similarity). {ECO:0000250}.
CC -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Probably by a type-
CC III secretion system. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; AJ225896; CAB38101.1; -; Genomic_DNA.
DR EMBL; AE006469; AAK65522.1; -; Genomic_DNA.
DR PIR; H95369; H95369.
DR RefSeq; NP_436110.1; NC_003037.1.
DR RefSeq; WP_010967830.1; NC_003037.1.
DR AlphaFoldDB; Q9Z3Q2; -.
DR SMR; Q9Z3Q2; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; AAK65522; AAK65522; SMa1587.
DR GeneID; 61599635; -.
DR KEGG; sme:SMa1587; -.
DR PATRIC; fig|266834.11.peg.897; -.
DR HOGENOM; CLU_031273_0_0_5; -.
DR OMA; AFKMGNG; -.
DR UniPathway; UPA00631; -.
DR Proteomes; UP000001976; Plasmid pSymA.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 2.150.10.10; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR001343; Hemolysn_Ca-bd.
DR InterPro; IPR011049; Serralysin-like_metalloprot_C.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR Pfam; PF00353; HemolysinCabind; 2.
DR SUPFAM; SSF49899; SSF49899; 1.
DR SUPFAM; SSF51120; SSF51120; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 3: Inferred from homology;
KW Exopolysaccharide synthesis; Glycosidase; Hydrolase; Plasmid;
KW Reference proteome; Repeat; Secreted.
FT CHAIN 1..465
FT /note="Endo-1,3-1,4-beta-glycanase EglC"
FT /id="PRO_0000075392"
FT REPEAT 33..50
FT /note="Hemolysin-type calcium-binding 1"
FT REPEAT 105..122
FT /note="Hemolysin-type calcium-binding 2"
FT REPEAT 123..140
FT /note="Hemolysin-type calcium-binding 3"
FT DOMAIN 213..462
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 349
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 354
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CONFLICT 52
FT /note="I -> T (in Ref. 1; CAB38101)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 465 AA; 49614 MW; 12CB879AED9E6558 CRC64;
MSRTVTNALG EPLSYGGSST AWFSASGSGP LLYGTAGNDS MWADSSVDVT MIGDSGDDIY
YLYSGVNRAS EAPSAGVDTI NTWMSYSLPE NFENLTVTGV EGFGFGNSAS NIISGGSGSQ
TINGGAGNDV LTGAGGADTF AFKRGNGSDL ISDFGSDDVV RLEGYGFTSF DHILANVAQE
GLDLKLSLAD GEYLVFANTS ADQLHANQFS LALDRSVLTQ TFSDDFNTLQ LSDGTSGVWD
PKYWWAPEKG ATLTGNDELQ WYVNPTYQPT ASANPFSVTD GVLTITAKPA SQAIQAETNG
YDYTSGMLTT YSSFAQTYGY FEMRADMPDD QGAWPAFWLL PGDGTWPPEL DVVEMHGQDP
NTVIATVHSN ETGSQTSIAS AARVTDTSGF HKYGVLWTEE EIVWYFDDAA IARADTPSDM
HDPMYMLVNL AIGGMAGPPT DGLMGGAEMK VDYVKAYSLD ADWHI
