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O82833 (GELLY_BACSP) Reviewed, UniProtKB/Swiss-Prot

Last modified December 11, 2013. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Gellan lyase

EC=4.2.2.25

Cleaved into the following 2 chains:

  1. N-terminal gellan lyase
  2. C-terminal gellan lyase
OrganismBacillus sp.
Taxonomic identifier1409 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length2475 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleaves the glycosidic bonds of gellan backbone and releases tetrasaccharide units of glucuronyl-glucosyl-rhamnosyl-glucose with unsaturated glucuronic acid at the non-reducing terminal. The enzyme is highly specific to the heteropolysaccharide gellan, especially deacetylated gellan. Ref.1 Ref.2

Catalytic activity

Eliminative cleavage of beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyluronate bonds of gellan backbone releasing tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-glucopyranosyluronic acid at the non-reducing end. The tetrasaccharide produced from deacetylated gellan is beta-D-4-deoxy-Delta(4)-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp. Ref.1 Ref.2 Ref.3

Subcellular location

Secreted.

Post-translational modification

Subject to proteolytic processing after secretion. Cleavage occurs between Gly-1205 and Leu-1206. This gives rise to a N-terminal gellan lyase of 130 kDa being the mature form of the gellan lyase. The function of C-terminal gellan lyase is not known.

Sequence similarities

Contains 1 cohesin domain.

Contains 1 fibronectin type-III domain.

Contains 1 NodB homology domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 6.0 in potassium phosphate and 7.5 in HEPES buffer. Ref.2

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionLyase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processpolysaccharide catabolic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncarbohydrate binding

Inferred from electronic annotation. Source: InterPro

hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds

Inferred from electronic annotation. Source: InterPro

lyase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 3535 Ref.1 Ref.2
Chain36 – 24752440Gellan lyase
PRO_0000424089
Chain36 – 12051170N-terminal gellan lyase
PRO_0000424090
Chain1206 – 24751270C-terminal gellan lyase
PRO_0000424091

Regions

Domain623 – 70886Fibronectin type-III
Domain1295 – 1518224NodB homology
Domain2111 – 2223113Cohesin
Compositional bias2024 – 210784Ala-rich

Sites

Site1205 – 12062Cleavage

Sequences

Sequence LengthMass (Da)Tools
O82833 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 0184ED2F01CAFDF2

FASTA2,475263,045
        10         20         30         40         50         60 
MRFSWKKLVS AALVMALLVG IVYPAASGRG AVASAASGTT VELVPTDDAF TSAVAKDANA 

        70         80         90        100        110        120 
NGTWMQLKGS IGGQRYIYMK FDLTALAGVE ADRIENAKVW LKKMGTNGTA MTVGLRAVDD 

       130        140        150        160        170        180 
TSWSESTLTW NNAPVYGSQV LSQQSVLSTP DVYYPFDLDE YLKTQLAAGK SKLAIAFVPI 

       190        200        210        220        230        240 
STLNENMEFY ARESTANTPK LVVELKDEPP APTGLMQLVQ SFGGHNKGHL RVVEFDATPA 

       250        260        270        280        290        300 
STTGNGTVGI TADGAAPAAA ADFPIALRFG TDGTIKAANA AGFESKTPVN YTAGQKYHVK 

       310        320        330        340        350        360 
AMINLSLGTY DLWLTPPNAG QPVLLAADYA FAASAPALND IGGVHATADA QSTDVPAVAN 

       370        380        390        400        410        420 
ARLIADHFVS KAPFKDEQGQ SLAIRLESDN SLANRSYAIK FDMNLTGNPL ETDALISYAD 

       430        440        450        460        470        480 
RSVTLNGFPD LAYIVRSNFG NFDVRNDNVY ASSHPSTAQS NRTYQVEVRI NPASGTGQPT 

       490        500        510        520        530        540 
RTYDVWIAPE GEQPVQLADQ FKARNYANTG YALNNIGQAF VYSQADGLLS IDNHVVQDGQ 

       550        560        570        580        590        600 
RLDEALARVN AASGEAAMTA ALESNALGLP MERYRLMDAA KRAQVAQDVL AGRPAEGYAH 

       610        620        630        640        650        660 
ALSVQAVFVS AVANRLDTEN PTAPANVQVA ISNTMQAHVS WTASSDDTGI LYYKVFRDGA 

       670        680        690        700        710        720 
LVGTVTNATS FVDNGLAPAT EYTYVVKAYD LVLKEAVSQP ATATSPGEQA QVRIPFSAEA 

       730        740        750        760        770        780 
IATAFGQPLL DYNLETHSGT LKWVMEWREE YEKSANALKL LTLLSASAPD YIGPDGVTTA 

       790        800        810        820        830        840 
SAKALQHLRS VTAGGNEPGF AGNGLSGQGY MPLLSAIVMA KKKAPAIWNA LTAAEKEKLD 

       850        860        870        880        890        900 
LMILAGLYGA KFAYDDENDN KTGIDATGNF DKEWNPNHRS GIAGAIMAMY YFEDAQWLND 

       910        920        930        940        950        960 
QMRSFNYDDW LARLTAAGLT NVRTIYQNSG KTLTEREIRK DAAGDGFVYK GHPLSQPGKI 

       970        980        990       1000       1010       1020 
MAEFVNYTFS HPVSPVGGFD SGIGKYRGYI VDGQDDLPNL GADSMGFEFD TLDANGKRSS 

      1030       1040       1050       1060       1070       1080 
LVYVFMGWKP NVDAITPVLL LDNIDSGLTS AETRDVVSRL SIGTTDMLYK NEHGYMTYAK 

      1090       1100       1110       1120       1130       1140 
GVNEGVKSLN GPILTINEEI WNRILNNPAA PMEAVNQASS AGQMRTALEA SALGMILYGY 

      1150       1160       1170       1180       1190       1200 
GALSETGKNA VAQHVLDARP AAGYANKAAA QNELYEGVRL QALLALSQAQ TAEQMRSALE 

      1210       1220       1230       1240       1250       1260 
SRALGLYKPK YETASQDKKQ FVAQYLLDNK PADGFLTKTE VREQVESALE PQGNQLRNLP 

      1270       1280       1290       1300       1310       1320 
PLASGEKRIN LADYDHWPQQ HGDAEVALWA DDKTGAFSLT IDDNFENEHD TWRSLAQQYG 

      1330       1340       1350       1360       1370       1380 
FKFSWFVITS LIKDPNKWRT LAAEGHEIGS HTVTHEDKGS TLDPAHLHSE YADSQALLNT 

      1390       1400       1410       1420       1430       1440 
IEGVRATTLA YPFGSGREDI AAEYYIAARG TVGLPNPADS INYMNTQSLS VRPGSLELTN 

      1450       1460       1470       1480       1490       1500 
QAANGNSVEA MVKTLVDPNH KVWSASYYRG WSNMLVHSLN ESGKTPSDGV TRTSRDLTQY 

      1510       1520       1530       1540       1550       1560 
LLTLLDTYRD QIWVGRYGDI VRYSQQRDTA HIVVTRKDDR KITFNLTDRM DDTLFDYPLT 

      1570       1580       1590       1600       1610       1620 
VKVRVDDAWS DIGATQAGEP IPFVETIRDG KRYLLVKAVP DKGSVSIVPD AASPLNVVNG 

      1630       1640       1650       1660       1670       1680 
AVTSEQMLSA IAAPGLGLDL GEFNALGAGK KRMVGSRLLE VRPADGYADA AALQDALDAA 

      1690       1700       1710       1720       1730       1740 
VEEANNAPSL SENASLSDLK VNGVTIAGFA PETYAYDIML PEGTTALPVV SFKVADTGKA 

      1750       1760       1770       1780       1790       1800 
TAVLQNAPAL PGTAKVTVTA EDNWTVATYT LRFQVRISAL QRVNTAPDAS AMRTAIENAA 

      1810       1820       1830       1840       1850       1860 
LGLVLAAYNG LTSEQKNSVA ASVLTHRPAT GYADVQAVQA ELNAALPKIN APLLAHAIVD 

      1870       1880       1890       1900       1910       1920 
QLNPDTVSTA NWTNLYGGTS GRKGGVYMKF NIASLAGLEA DAIGDAKVQF FTTREGTVIG 

      1930       1940       1950       1960       1970       1980 
YAAPSSWEAP LTWNTQPLAD LKNSNMAALA EIGRTAVQAT GANYEMNITQ YVKDAAAADK 

      1990       2000       2010       2020       2030       2040 
TELSLVLLGS NNTNITMQKI PTAFALSVTL ATYGEPNPEP SPLAAVNEAG DAAAMQGAIA 

      2050       2060       2070       2080       2090       2100 
AVELDLNLTA YNGLTAAQRI DVAQALLDNR PAAGYAHALA VQVALDAAVA AAQPANQAPG 

      2110       2120       2130       2140       2150       2160 
GTLAASAEQL QPGQQLELTV GVSDASRFTG ADILVHYDPQ ALTFATELYE GVRMLKAEAI 

      2170       2180       2190       2200       2210       2220 
ASLQANYQVA AAMAEQPGTI KILLFTAGAG QPLSGTLPLF KLRASVKDDA QTGVSTAVSL 

      2230       2240       2250       2260       2270       2280 
SDFELTFEGE DSVWPDTTRA AVSLQIAAHP VEADKTALIA KIAHAQALLT GATVGANPGQ 

      2290       2300       2310       2320       2330       2340 
YPQAAYDALA DAIGLAEEKR DLTGVSQAAV DEAVASLGTA EQQFLNAVIP GVPADLTALN 

      2350       2360       2370       2380       2390       2400 
AAIAKAQRLH DNGPYGEKIG QYPQSAKVPL KSALDAAKAV GGSGASSQES VNAAAASLNG 

      2410       2420       2430       2440       2450       2460 
AIQTFERSLV TLVGGGATKV GIRDLSIVAK YYGVTSSDPN WGKVSAAAID GGNEITIEVL 

      2470 
AAVARMILAD WAAGQ 

« Hide

References

[1]"Polysaccharide lyase: molecular cloning of gellan lyase gene and formation of the lyase from a huge precursor protein in Bacillus sp. GL1."
Hashimoto W., Sato N., Kimura S., Murata K.
Arch. Biochem. Biophys. 354:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-45, FUNCTION, CATALYTIC ACTIVITY.
Strain: GL1.
[2]"Posttranslational processing of polysaccharide lyase: maturation route for gellan lyase in Bacillus sp. GL1."
Miyake O., Kobayashi E., Nankai H., Hashimoto W., Mikami B., Murata K.
Arch. Biochem. Biophys. 422:211-220(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 36-41; 1169-1194 AND 1203-1205, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PROTEOLYTIC PROCESSING.
Strain: GL1.
[3]"Microbial system for polysaccharide depolymerization: enzymatic route for gellan depolymerization by Bacillus sp. GL1."
Hashimoto W., Maesaka K., Sato N., Kimura S., Yamamoto K., Kumagai H., Murata K.
Arch. Biochem. Biophys. 339:17-23(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: CATALYTIC ACTIVITY.
Strain: GL1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB006853 Genomic DNA. Translation: BAA29068.1.
PIRT00047.

3D structure databases

ProteinModelPortalO82833.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16405.

Family and domain databases

Gene3D2.60.40.10. 1 hit.
3.20.20.370. 1 hit.
InterProIPR002102. Cohesin_dom.
IPR003961. Fibronectin_type3.
IPR011330. Glyco_hydro/deAcase_b/a-brl.
IPR013783. Ig-like_fold.
IPR002509. Polysac_deacetylase.
[Graphical view]
PfamPF00963. Cohesin. 1 hit.
PF00041. fn3. 1 hit.
PF01522. Polysacc_deac_1. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
[Graphical view]
SUPFAMSSF49265. SSF49265. 1 hit.
SSF88713. SSF88713. 1 hit.
PROSITEPS50853. FN3. 1 hit.
PS51677. NODB. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGELLY_BACSP
AccessionPrimary (citable) accession number: O82833
Entry history
Integrated into UniProtKB/Swiss-Prot: October 16, 2013
Last sequence update: November 1, 1998
Last modified: December 11, 2013
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families