NDVB_RHIME
ID NDVB_RHIME Reviewed; 2832 AA.
AC P20471;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 02-NOV-2001, sequence version 2.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Cyclic beta-(1,2)-glucan synthase NdvB {ECO:0000303|PubMed:2154461};
DE EC=2.4.1.- {ECO:0000305|PubMed:8830704};
GN Name=ndvB {ECO:0000303|PubMed:2154461}; OrderedLocusNames=R03286;
GN ORFNames=SMc04382;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, DISRUPTION PHENOTYPE, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2154461; DOI=10.1016/s0021-9258(19)39878-3;
RA Ielpi L., Dylan T., Ditta G.S., Helinski D.R., Stanfield S.W.;
RT "The ndvB locus of Rhizobium meliloti encodes a 319-kDa protein involved in
RT the production of beta-(1-->2)-glucan.";
RL J. Biol. Chem. 265:2843-2851(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481430; DOI=10.1073/pnas.161294398;
RA Capela D., Barloy-Hubler F., Gouzy J., Bothe G., Ampe F., Batut J.,
RA Boistard P., Becker A., Boutry M., Cadieu E., Dreano S., Gloux S.,
RA Godrie T., Goffeau A., Kahn D., Kiss E., Lelaure V., Masuy D., Pohl T.,
RA Portetelle D., Puehler A., Purnelle B., Ramsperger U., Renard C.,
RA Thebault P., Vandenbol M., Weidner S., Galibert F.;
RT "Analysis of the chromosome sequence of the legume symbiont Sinorhizobium
RT meliloti strain 1021.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9877-9882(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, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=8830704; DOI=10.1128/jb.178.20.6043-6048.1996;
RA Castro O.A., Zorreguieta A., Ielmini V., Vega G., Ielpi L.;
RT "Cyclic beta-(1,2)-glucan synthesis in Rhizobiaceae: roles of the 319-
RT kilodalton protein intermediate.";
RL J. Bacteriol. 178:6043-6048(1996).
CC -!- FUNCTION: Involved in the biosynthesis of cyclic beta-(1,2)-glucan
CC (PubMed:2154461, PubMed:8830704). It seems that NdvB is involved in
CC three enzymatic activities. First, it may catalyze the transfer of the
CC first glucose from UDP-Glc to an unknown amino acid (PubMed:8830704).
CC In the second enzymatic activity (UDP-Glc:beta-(1,2) oligosaccharide
CC glucosyltransferase), it may be responsible for chain elongation
CC (PubMed:8830704). Finally, in the third activity, it may catalyze
CC glucan cyclization and release from the protein (PubMed:8830704). NdvB
CC is also involved in nodule invasion and in bacteroid development
CC (PubMed:2154461). {ECO:0000269|PubMed:2154461,
CC ECO:0000269|PubMed:8830704}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[(1->2)-beta-D-glucosyl](n) + UDP-alpha-D-glucose = [(1->2)-
CC beta-D-glucosyl](n+1) + H(+) + UDP; Xref=Rhea:RHEA:53084, Rhea:RHEA-
CC COMP:11881, Rhea:RHEA-COMP:13458, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:27517, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885;
CC Evidence={ECO:0000305|PubMed:8830704};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255,
CC ECO:0000305|PubMed:2154461, ECO:0000305|PubMed:8830704}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to produce
CC cyclic beta-(1,2)-glucan and produce white ineffective nodules on
CC alfalfa plant. {ECO:0000269|PubMed:2154461}.
CC -!- SIMILARITY: Belongs to the NdvB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26305.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; J05219; AAA26305.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL591688; CAC47865.1; -; Genomic_DNA.
DR PIR; A35548; A35548.
DR RefSeq; NP_387392.1; NC_003047.1.
DR SMR; P20471; -.
DR STRING; 266834.SMc04382; -.
DR CAZy; GH94; Glycoside Hydrolase Family 94.
DR CAZy; GT84; Glycosyltransferase Family 84.
DR PRIDE; P20471; -.
DR EnsemblBacteria; CAC47865; CAC47865; SMc04382.
DR KEGG; sme:SMc04382; -.
DR PATRIC; fig|266834.11.peg.4845; -.
DR eggNOG; COG3459; Bacteria.
DR HOGENOM; CLU_000646_0_0_5; -.
DR OMA; FEYLMPL; -.
DR PRO; PR:P20471; -.
DR Proteomes; UP000001976; 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:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11756; GH94N_ChvB_NdvB_1_like; 1.
DR CDD; cd11753; GH94N_ChvB_NdvB_2_like; 1.
DR Gene3D; 1.50.10.10; -; 1.
DR Gene3D; 2.70.98.40; -; 2.
DR InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR InterPro; IPR009342; Carb-bd_put_dom.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR033432; GH36_catalytic.
DR InterPro; IPR037824; GH94N_2_NdvB.
DR InterPro; IPR037820; GH94N_NdvB.
DR InterPro; IPR037018; Glyco_hydro_65_N_sf.
DR InterPro; IPR010383; Glyco_hydrolase_94.
DR InterPro; IPR019282; Glycoamylase-like_cons_dom.
DR Pfam; PF17167; Glyco_hydro_36; 1.
DR Pfam; PF06165; Glyco_transf_36; 2.
DR Pfam; PF10091; Glycoamylase; 1.
DR SMART; SM01068; CBM_X; 2.
DR SUPFAM; SSF48208; SSF48208; 1.
DR SUPFAM; SSF74650; SSF74650; 2.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Glycosyltransferase; Membrane;
KW Nodulation; Reference proteome; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..2832
FT /note="Cyclic beta-(1,2)-glucan synthase NdvB"
FT /id="PRO_0000096773"
FT TRANSMEM 411..431
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 831..851
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 880..900
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 938..958
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 959..979
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 1299..1506
FT /note="Glycoamylase-like"
FT /evidence="ECO:0000255"
FT CONFLICT 47
FT /note="T -> A (in Ref. 1; AAA26305)"
FT /evidence="ECO:0000305"
FT CONFLICT 1187
FT /note="L -> F (in Ref. 1; AAA26305)"
FT /evidence="ECO:0000305"
FT CONFLICT 2602
FT /note="D -> G (in Ref. 1; AAA26305)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2832 AA; 315751 MW; 171EA89F03A936F2 CRC64;
MLQNTTQSNL PREPEAKQID YNDSIRSTYF SIDDLRACGA SLAEKGTSAL PGFFPFEFRA
RHRENEKEIL RVYRATAADV EAGASITPAA EWLLDNHHVV EEAIQEVRRD FPRRFYRQLP
TLSVSGTVIP RTMALAWLYV AHTHSTVTRE SITAMVEGFQ EHETLKIGEL WALPSILRFV
LIENLRRIAI RVERSRGMRR KANEVADQLI RLNDPEGCRT LLVESEALAA DNTFIAQLLY
RMRDGSQSSG AVIAWIEERL ERRGTDVEEA LVAEQNRLSS GNATMSNIIR SLREIDDTDW
AVWFESVSKI DATLREGSDY AALDFGSRNT YRDTIEKLAR RSGHSEHEVT EIAIEMVEEA
KAAAAVEAPL QEPNVGSFLV GKQRLALEKR IGYSPSIFQH LIRSVRKLDW FAIAGPNILL
TILAMIVVYA FVSPMDIPSG AKLIMLLLFA LPASEGAMGL FNTVFTLFAK PSRLVGYEFL
DGIPEDARTL VVVPCLIAKR DHVDELVRNL EVHYLANPRG EIYFALLSDW ADSKSEEAPA
DTDVLEYAKR EIASLSARYA YDGKTRFFLL HRRRLYNEAE GVWMGWERKR GKLHELNLLL
RGDRDTSFLQ GANMVPEGVQ YVMTLDSDTR LMRDAVTKLV GKLYHPINRP VVNPRTQEVV
TGYSLLQPRV TPSLTTGSEA SAFQRIFTIN RGIDPYVFTV SDVYQDIAGE GSFTGKGLYH
VDAFEAALKS RIEENAVLSH DLLEGSYARC ALVTDIELVE DFPIRYEVEM SRQHRWARGD
WQLLPYIFNP KNGLSMLGRW KMYDNLRRSL IPVAWLAASV MGWYYMEPTP ALIWQLVLIF
SLFVAPTLSL ISGIMPRRND IVARAHLHTV LSDIRAANAQ VALRIVFIAH NAAMMADAIV
RSLYRTFVSR KLMLEWRTAA QVQSAGHGSI GDYFRAMWTA PALALVSLAL AAISDTGLPF
IGLPFALIWA ASPAVAWFVS QSAETEDQLV VSEEAIEEMR KIARRTWRYF EAFVTAEQNF
LPPDNFQETP QPVLAERTSP TNIGVYLLSV MSARSFGWIG FEETITRLEQ TIATIDRMPK
YRGHLFNWYR TRGLEPMEPR YVSSVDSGNL AGHLIAVSSM CREWAEAPSA HVQGNLDGIG
DVAAILKEAL NELPDDRKTV RPLRRLVEER IAGFQNALAA VKRERELASI RVINLAVLAR
DMHKLTVNLD HEVRTVQSGE VATWAGSLVA ACEAHIADGV FDLGAIEALR QRLLVLKERA
RDIAFSMDFS FLFRPERRLL SIGYRVNANE LDEACYDLLA SEARLTSLFA IAKGDLPTEH
WYKLGRPIVP IGARGALVSW SGSMFEYLMP PLVMQERQGG ILNQTNNLVV QEQINHGRRL
GTPWGISEAA FNARDHELTY QYTNFGVPTL GLKRGLGQNA VIAPYASILA CMYDPKSALA
NLARLREVGA LGAYGYHDAV DFTPTRVPEG QKCAVVRNYY AHHHGMSVAA VANVVFNGQL
REWFHADPVI EAAELLLQEK APRDIPVMAA KREPEALGKG QADLLRPEVR VVEDPINQDR
ETVLLSNGHY SVMLTATGAG YARWNGQSVT RWTPDPVEDR TGTFIFLRDT VTGDWWSATA
EPRRAPGEKT VTRFGDDKAE FVKTVGDLTS EVECIVATEH DAEGRRVILL NTGTEDRFIE
VTSYAEPVLA MDDADSSHPT FSKMFLRTEI SRHGDVIWVS RNKRSPGDPD IEVAHLVTDN
AGSERHTQAE TDRRRFLGQG RTLAEAAAFD PGATLSGTDG FTLDPIVSLR RVVRVPAGKK
VSVIFWTIAA PDREGVDRAI DRYRHPETFN HELIHAWTRS QVQMRHVGIT SKEAASFQML
GRYLVYPDMH LRADAETVKT GLASQSALWP LAISGDFPIF CLRINDDGDL GIAREALRAQ
EYLRARGITA DLVVVNERAS SYAQDLQHTL DSMCENLRLR GLSDGPRQHI FAVRRDLMEP
ETWSTLISAS RAVFHARNGT ISDQIARATS LYSKSSEKKE EGAEMLLPVI READARTAVE
LDGGDLDFWN GFGGFAEDGR EYAVRLRGGE ATPQPWINVI SNEQFGFHVS AEGAAFSWSR
NSRDYQLTPW TNDAVVNRPG EAIFVRDMAS GAVLTPYAAL SRRKSALFET RHGLGYSRFL
STQDELEIEA MHTVHRTLPA KLVRLTIRNR SSAARKLRVY GYAEWVLGNN RSRTAPFVLS
EWDESAKTLV ATNPYSIDYP GRCAFFASDG DIAGYTASRR EFLGRAGGIL APQAVISGAE
LTGSTDVDGD ACAALATDIT VEAGVERQVT FFLGDADNPD QVRAVLEELR ADSFGAALEA
AKAFWGDFTG VVKVETPDRA FNHMINHWLP YQALGCRIMA RSAFYQASGA FGFRDQLQDT
LAFLIHRPAL ARAQILNAAA RQFVEGDVQH WWLPGTDAGV RTMISDDVVW LAHAVAHYCA
VTGEEDILKE KVPFITGPAL EEGQHDSFYK PDVADEVGDV YEHCARALDL AIHRTGANGL
PLILGGDWND GMNRVGEAGE GTSVWLGWFL AGTLRAFLPY ARARKDKPRV ALWERHLEAL
KDALEQAGWD GDYYRRGYYD DDTPLGSAEN GECRIDSIAQ SWSTLSGEGD KERSLRAMDA
VMAELVDPEK RIVRLFTPPL ETTKQDPGYI KAYPPGVREN GGQYTHAATW VVLAFAAQER
AEEAWRTFRM LNPVSHALSQ VDAEHYRVEP YVVAADIYGE GALAGRGGWT WYTGSAGWLY
RAGVEGILGI RKRGDKLLIR PVLPSEWPGY SAEVRVNGTT HRISVSRDSK SGEPVVSVNN
SVTKNAHEGV LL
