EXSH_RHIME
ID EXSH_RHIME Reviewed; 465 AA.
AC O33680;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Endo-1,3-1,4-beta-glycanase ExsH;
DE EC=3.2.1.-;
DE AltName: Full=Succinoglycan biosynthesis protein ExsH;
GN Name=exsH; OrderedLocusNames=RB1055; ORFNames=SMb20932;
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], FUNCTION, AND SUBCELLULAR LOCATION.
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 [2]
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 [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).
RN [4]
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:11902715,
CC ECO:0000269|PubMed:9560202}. Note=Secreted by a type I secretion system
CC composed of PrsD and PrsE.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family. {ECO:0000305}.
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DR EMBL; U89164; AAB64093.1; -; Genomic_DNA.
DR EMBL; AL591985; CAC49455.1; -; Genomic_DNA.
DR PIR; G95973; G95973.
DR RefSeq; NP_437595.1; NC_003078.1.
DR RefSeq; WP_010975894.1; NC_003078.1.
DR AlphaFoldDB; O33680; -.
DR SMR; O33680; -.
DR STRING; 266834.SM_b20932; -.
DR CAZy; GH16; Glycoside Hydrolase Family 16.
DR EnsemblBacteria; CAC49455; CAC49455; SM_b20932.
DR GeneID; 61601014; -.
DR KEGG; sme:SM_b20932; -.
DR PATRIC; fig|266834.11.peg.5984; -.
DR eggNOG; COG2273; Bacteria.
DR eggNOG; COG2931; Bacteria.
DR HOGENOM; CLU_031273_0_0_5; -.
DR OMA; TGDDIYY; -.
DR UniPathway; UPA00631; -.
DR Proteomes; UP000001976; Plasmid pSymB.
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 1: Evidence at protein level;
KW Exopolysaccharide synthesis; Glycosidase; Hydrolase; Plasmid;
KW Reference proteome; Repeat; Secreted.
FT CHAIN 1..465
FT /note="Endo-1,3-1,4-beta-glycanase ExsH"
FT /id="PRO_0000075391"
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 206..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"
SQ SEQUENCE 465 AA; 50286 MW; 6C8482366E9E8CA8 CRC64;
MSKTVLNAVG TPLYYSGSST AWFSATGSGP TLHGTAGNDS MWGDSSVNVT MIGGRGDDIY
YLYSSINRAY EAAGEGVDTI STWMSYTLPA NFENLTVTGS GRFAFGNEAD NIIKGGSGTQ
TIDGRGGNDV LIGAGGADTF VFARGNGSDL ITDFNYDDIV RLDGYGFTSF EQILSNVAQE
GADLRLHLAD GESLVFANTT ADELQAHQFR LSLDRSVLSQ TFSDEFNTLQ LRNGTSGVWD
AKFWWAPEKG ATLSSNGEQQ WYINPSYEPT ASVNPFSVNN GVLTITAAPA SEAIQAEING
YDYTSGMLTT YSSFAQTYGY FEMRADMPDD QGVWPAFWLL PADGSWPPEL DVVEMRGQDS
NTVIATVHSN ETGSRTSIEN SVKVADASGF HTYGVLWTEE EIVWYFDDAA IARADTPSDM
HDPMYMLVNL AVGGIAGTPR DGLADGSEMK IDYIKAYSLD ADWQI
