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   04-NOV-2026, entry version 138.
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; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; 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) + UDP + H(+); 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; WP_010970544.1; NC_003047.1.
DR   SMR; 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; AACMMTD; -.
DR   OrthoDB; 9769991at2; -.
DR   PRO; PR:P20471; -.
DR   Proteomes; UP000001976; Chromosome.
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   FunFam; 1.50.10.140:FF:000003; Cyclic beta-1,2-glucan synthase; 1.
DR   FunFam; 2.70.98.40:FF:000007; Cyclic beta-1,2-glucan synthase; 1.
DR   Gene3D; 1.50.10.10; -; 1.
DR   Gene3D; 1.50.10.140; -; 2.
DR   Gene3D; 2.70.98.40; Glycoside hydrolase, family 65, N-terminal domain; 2.
DR   Gene3D; 2.60.420.10; Maltose phosphorylase, domain 3; 1.
DR   InterPro; IPR008928; 6-hairpin_glycosidase_sf.
DR   InterPro; IPR012341; 6hp_glycosidase-like_sf.
DR   InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR   InterPro; IPR037018; GH65_N.
DR   InterPro; IPR033432; GH94_catalytic.
DR   InterPro; IPR052047; GH94_Enzymes.
DR   InterPro; IPR037824; GH94N_2_NdvB.
DR   InterPro; IPR037820; GH94N_NdvB.
DR   InterPro; IPR010383; Glyco_hydrolase_94_b-supersand.
DR   InterPro; IPR019282; Glycoamylase-like_cons_dom.
DR   PANTHER; PTHR37469:SF2; CELLOBIONIC ACID PHOSPHORYLASE; 1.
DR   PANTHER; PTHR37469; CELLOBIONIC ACID PHOSPHORYLASE-RELATED; 1.
DR   Pfam; PF06165; GH94_b-supersand; 2.
DR   Pfam; PF17167; Glyco_hydro_94; 1.
DR   Pfam; PF10091; Glycoamylase; 1.
DR   SMART; SM01068; CBM_X; 2.
DR   SUPFAM; SSF74650; Galactose mutarotase-like; 2.
DR   SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
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
//