EXOK_RHIME
ID EXOK_RHIME Reviewed; 269 AA.
AC P33693;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, sequence version 1.
DT 25-MAY-2022, entry version 120.
DE RecName: Full=Endo-1,3-1,4-beta-glycanase ExoK;
DE EC=3.2.1.-;
DE AltName: Full=Succinoglycan biosynthesis protein ExoK;
DE Flags: Precursor;
GN Name=exoK; OrderedLocusNames=RB1080; ORFNames=SMb20955;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=8226645; DOI=10.1128/jb.175.21.7033-7044.1993;
RA Glucksmann M.A., Reuber T.L., Walker G.C.;
RT "Family of glycosyl transferases needed for the synthesis of succinoglycan
RT by Rhizobium meliloti.";
RL J. Bacteriol. 175:7033-7044(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=RCR2011 / SU47;
RX PubMed=8479421; DOI=10.1007/bf00279541;
RA Becker A., Kleickmann A., Arnold W., Puehler A.;
RT "Analysis of the Rhizobium meliloti exoH/exoK/exoL fragment: ExoK shows
RT homology to excreted endo-beta-1,3-1,4-glucanases and ExoH resembles
RT membrane proteins.";
RL Mol. Gen. Genet. 238:145-154(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [4]
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).
RN [5]
RP FUNCTION.
RC STRAIN=1021;
RX PubMed=11902715; DOI=10.1046/j.1365-2958.1997.4481804.x;
RA York G.M., Walker G.C.;
RT "The Rhizobium meliloti exoK gene and prsD/prsE/exsH genes encode
RT components of independent degradative pathways which contribute to
RT production of low-molecular-weight succinoglycan.";
RL Mol. Microbiol. 25:117-134(1997).
RN [6]
RP FUNCTION, PATHWAY, SUBCELLULAR LOCATION, AND CHARACTERIZATION.
RC STRAIN=1021;
RX PubMed=9560202; DOI=10.1073/pnas.95.9.4912;
RA York G.M., Walker G.C.;
RT "The Rhizobium meliloti ExoK and ExsH glycanases specifically depolymerize
RT nascent succinoglycan chains.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:4912-4917(1998).
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.
CC {ECO:0000269|PubMed:11902715, ECO:0000269|PubMed:9560202}.
CC -!- PATHWAY: Glycan metabolism; exopolysaccharide biosynthesis.
CC {ECO:0000269|PubMed:9560202}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9560202}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; L20758; AAA16048.1; -; Unassigned_DNA.
DR EMBL; Z17219; CAA78927.1; -; Genomic_DNA.
DR EMBL; AL591985; CAC49480.1; -; Genomic_DNA.
DR PIR; H95976; H95976.
DR PIR; S34804; S34804.
DR RefSeq; NP_437620.1; NC_003078.1.
DR RefSeq; WP_010975917.1; NC_003078.1.
DR AlphaFoldDB; P33693; -.
DR SMR; P33693; -.
DR STRING; 266834.SM_b20955; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; CAC49480; CAC49480; SM_b20955.
DR GeneID; 25013379; -.
DR GeneID; 61601035; -.
DR KEGG; sme:SM_b20955; -.
DR PATRIC; fig|266834.11.peg.6008; -.
DR eggNOG; COG2273; Bacteria.
DR HOGENOM; CLU_071026_0_0_5; -.
DR OMA; WYVSDGW; -.
DR UniPathway; UPA00631; -.
DR PRO; PR:P33693; -.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 InterPro; IPR044791; Beta-glucanase/XTH.
DR InterPro; IPR008264; Beta_glucanase.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000757; GH16.
DR InterPro; IPR008263; GH16_AS.
DR PANTHER; PTHR31062; PTHR31062; 1.
DR Pfam; PF00722; Glyco_hydro_16; 1.
DR PRINTS; PR00737; GLHYDRLASE16.
DR SUPFAM; SSF49899; SSF49899; 1.
DR PROSITE; PS01034; GH16_1; 1.
DR PROSITE; PS51762; GH16_2; 1.
PE 1: Evidence at protein level;
KW Exopolysaccharide synthesis; Glycosidase; Hydrolase; Plasmid;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..269
FT /note="Endo-1,3-1,4-beta-glycanase ExoK"
FT /id="PRO_0000011799"
FT DOMAIN 40..252
FT /note="GH16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT ACT_SITE 138
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
FT ACT_SITE 142
FT /note="Proton donor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10064"
SQ SEQUENCE 269 AA; 30084 MW; 073CC7ED65EF2611 CRC64;
MTIDRYRRFA RLAFIATLPL AGLATAAAAQ EGANGKSFKD DFDTLDTRVW FVSDGWNNGG
HQNCTWSKKQ VKTVDGILEL TFEEKKVKER NFACGEIQTR KRFGYGTYEA RIKAADGSGL
NSAFFTYIGP ADKKPHDEID FEVLGKNTAK VQINQYVSAK GGNEFLADVP GGANQGFNDY
AFVWEKNRIR YYVNGELVHE VTDPAKIPVN AQKIFFSLWG TDTLTDWMGT FSYKEPTKLQ
VDRVAFTAAG DECQFAESVA CQLERAQSE
