ID Q2YNV7_BRUA2 Unreviewed; 2732 AA.
AC Q2YNV7;
DT 20-DEC-2005, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2005, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE SubName: Full=Cyclic beta 1-2 glucan synthetase {ECO:0000313|EMBL:CAJ10064.1};
GN OrderedLocusNames=BAB1_0108 {ECO:0000313|EMBL:CAJ10064.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391 {ECO:0000313|EMBL:CAJ10064.1, ECO:0000313|Proteomes:UP000002719};
RN [1] {ECO:0000313|EMBL:CAJ10064.1, ECO:0000313|Proteomes:UP000002719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 {ECO:0000313|EMBL:CAJ10064.1,
RC ECO:0000313|Proteomes:UP000002719};
RX PubMed=16299333; DOI=10.1128/IAI.73.12.8353-8361.2005;
RG Microbial Genomics Group;
RG Lawrence Livermore National Laboratory;
RG and the Genome Analysis Group;
RG Oak Ridge National Laboratory;
RA Chain P., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
CC -!- INTERACTION:
CC Q2YNV7; Q2YQ73: ndvA; NbExp=5; IntAct=EBI-11509311, EBI-11509336;
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DR EMBL; AM040264; CAJ10064.1; -; Genomic_DNA.
DR IntAct; Q2YNV7; 2.
DR STRING; 359391.BAB1_0108; -.
DR CAZy; GH94; Glycoside Hydrolase Family 94.
DR CAZy; GT84; Glycosyltransferase Family 84.
DR KEGG; bmf:BAB1_0108; -.
DR HOGENOM; CLU_000646_0_0_5; -.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0060187; C:cell pole; IDA:AgBase.
DR GO; GO:0005737; C:cytoplasm; IDA:AgBase.
DR GO; GO:0005886; C:plasma membrane; IDA:AgBase.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0043621; F:protein self-association; IPI:AgBase.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 1.50.10.140; -; 1.
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; IPR009342; Carb-bd_put_dom.
DR InterPro; IPR021478; DUF3131.
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 PANTHER; PTHR37469:SF2; CELLOBIONIC ACID PHOSPHORYLASE; 1.
DR PANTHER; PTHR37469; CELLOBIONIC ACID PHOSPHORYLASE-RELATED; 1.
DR Pfam; PF11329; DUF3131; 1.
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; SSF74650; Galactose mutarotase-like; 2.
DR SUPFAM; SSF48208; Six-hairpin glycosidases; 1.
PE 1: Evidence at protein level;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002719};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 282..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 318..343
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 686..704
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 711..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 761..782
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 803..825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 831..852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 916..934
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1410..1468
FT /note="Putative carbohydrate binding"
FT /evidence="ECO:0000259|SMART:SM01068"
FT DOMAIN 1941..2005
FT /note="Putative carbohydrate binding"
FT /evidence="ECO:0000259|SMART:SM01068"
FT COILED 1037..1095
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 2732 AA; 305243 MW; 1B9B46005851838E CRC64;
MPRIFALAWL YVAHTDSNFS LKMLTAMVKG FQTVEPLKIG ELWALPSAVR YFLIENARRL
AMRVDRAREM RNLANTAADR IVVAAEGAEL DGILAQYASA ACDSTFATHL LYRLRSSSTD
TTAAASWLER ILEQDGSNPE DAIIEEHARQ STGGVTMGNV IRSLKSIDDV DWETWFETVN
EVDAILRDHS DFELLDFRSR NAYRVTIEKL ARYSDMSEID ITWAALKLAE DGSRAEKAGH
PEAEGKGAIS YYLSGEGRRD LEKVCGYRAP FGVKALRLYR GLGLWGLFVP TAIFTVLTLL
LVNYCMMRAG LSTDLRTLFT LLAIFPAMDA SYSLFNVLVP WFVQPTRLIG FEYKDGLPPE
ARTLVAVPTF ITSRDSIDEQ IRNLEVHYLT NPRGEIYFAL VSDWTDASQE IVPADMEIYE
YARDEIAKLN EHYTGDDQPR FFLLHRRRLF NEKQGCWMGW ERKRGKLHEL NLLLRGDQDT
SFFPADERLP KDIKYVMTLD ADTRLTPEAV THLAGKLNHP MNRPVIDEKT GKVVRGYGIL
QPRVTPSLTT GDEASFLQRV FSVNRGIDPY VFAVSDTYQD LLGEGTFTGK GLYDIDAFEA
ALKGRVPENT LLSHDLLEGG YARSALVSDV EVVEDYPTGY NVDVSRHHRW ARGDWQLLPW
LFSTGRGVSA ITRWKMVDNL RRSLNPILWL IAAIVGWSVL PLGAAAVWQG FLILSMFVAP
TFGIVTNLIP ASMDYSLKGH AQSVLTDIAL GTADVALRTT FIAHSAFLMA DAIARTIYRL
FISRRNLLEW RTAAQARTSP DTLLFYFQLM WPAMAIAGLA IFFPLAAESH AALIAAPFVV
IWFASPLIAW LVSRSAKPQD TLEVLSSDKA DLRRYARRTW RYFAEFANEE NNHLPPDNFQ
EDPAPIVAQR TSPTNIGVYL LSVIAARDFG WIGFDETLDR VEATLGSLDK MEKYQGHLYN
WYETNTLNPM RPLYVSAVDS GNLAGHLVTL SSALEEWAEA PSVYVQGDLD GIIDVNDILE
ETIARIPDDR RVLRPLRRRL EERIANFRRA VTSIKDEPET ASFRTINLSL FASDIVRLMD
ELDSEVETVA SAEAREWARI LVDTCKAHTD DAIGEHDTDA LRERLRDLAT RARQLAFDMQ
FGFLERKERR LLSIGFRVQE NELDESCYDL LASEARLASL FAIAKGDVPV EHWFKLGRLL
VPVGWKGALL SWSGSMFEYL MPPLVMSEPL GSLLDQTNKL VVQRQIDYAT SRDLPWGISE
AAFNARDAHL NYQYSNFGVP NLGLQRGLSR NAVIAPYASL LAAQYQPAAA VANLKRLAKL
GALGRYGFHD SVDFTPSRIR EGETCAVVKN YYAHHHGMSI IAVNNVIFEG RMRERFHNDP
VIEAAELLLQ EKAPREIPMI YAKTENPMRV DSGGFDDAPM RIIDKPFRAP RTTHMMSNGQ
YALMVTANGS GYSRWHNWDI TRFHADASED MQGTFLFLRD MESGYWWSAT GEPVRNPDEE
TKTVFTEDKA EFYKTAGDIK TVMEVIVASE ADGEGRRLDI INTSPRDRMI EVTSYAELVL
NDSDSDAAHP AFAKMFVETE IADSGSTIYA KRRKRAPSAP DIHAAHFVTD LSGALREIEV
ETDRRAFIGR GRSLRNAAAF DPGAKFTGSQ GCVLDPIVSV RTRVRVPAHK KVSLVFWTFA
GGSRDAVEHA VTMHRHPETF AREYSLSWTS SQVQLYHIGI KPAEAADYQK VAAYLLYPER
TLRQPPETIA SGLGKQSDLW PMSISGDYPI FALRIDNEAD LDVLRGVLRA QEYWRSKGLI
VDVVAVNERA FSYAQDTQRA IDWIVEGFRA RGGGQPHIFA VRRDQMSEES YNTLLASARI
VMHAQNGSLA EQLRRSEEIT VDLAARSDAR TATNGQASVQ GLGAAGLAPV AIERGAEERR
PVVKPPVDRP RPSGDDLRFW NGYGGFAEDG SYVVRINGRT STPHPWINVI ANPSFGFHVS
AEGSAFTWAG NSRDYQLTPW ANDPVTNRPG EAIYILDRET GRSFAPTANV LRDEAVTYEA
RHGHGYSAFS AQHGELALEL THIVDAEKPV RLSRLTITNK GRSKRKLRVY GYVEWVLGNA
RARNVPFIVP SQDEELGALF AGNPYHPDKS GQVAFFAASE KPQSVTADRG EFIGTAGSVD
RPEIVLAGKV LSGTVEAGRD PCAALALDIE VGPGEAREIV FLLGNTADQK QAKALIADMR
TASFEEKLVA ARHQWESFFN RVQVKTPDPA FDLMVNGWLP YQAVACRIWA RAAFYQVSGA
FGFRDQLQDT LSLLLVDPSL AREQILNAAS RQFREGDVQH WWLPATGAGV RTLISDDVVW
LGYGASLYVE TTGDRFILDE KLPFLEGRKL EEGEHDAFYE PEISKETASL YEHCALALDL
AVARTGKHGL PLILGGDWND GMNLVGVKGK GESVWLGWFL AYTLKAFIPL AEARKDQKRA
DLWKAHVESL TAALDRDGWD GEWYRRGFYD NGRPLGSKNS DECQIDAIAQ SWSVLSGVAD
PKRAKKAMAS LEKYLLDEDN ALLRLFTPPF DVTPQEPGYI KGYPPGVREN GGQYTHGATW
AILALARMGK AAEAWRLFSL ISPVSHGRNP DVYRVEPYVI AADIYSVAPR CGQGGWTWYT
GSAGWFYRVA TEGILGVTKR GDRLHFQPAL PPEWEGYEAE LRFGEALYRV KVVAGAKAGT
IRLNGRKLAK PDEGVALKPY GEHEIVVELP KQ
//
