ID   GELLY_BACSP             Reviewed;        2475 AA.
AC   O82833;
DT   16-OCT-2013, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Gellan lyase;
DE            EC=4.2.2.25;
DE   Contains:
DE     RecName: Full=N-terminal gellan lyase;
DE   Contains:
DE     RecName: Full=C-terminal gellan lyase;
DE   Flags: Precursor;
OS   Bacillus sp.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1409;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 36-45, FUNCTION, AND
RP   CATALYTIC ACTIVITY.
RC   STRAIN=GL1;
RX   PubMed=9633595; DOI=10.1006/abbi.1998.0674;
RA   Hashimoto W., Sato N., Kimura S., Murata K.;
RT   "Polysaccharide lyase: molecular cloning of gellan lyase gene and formation
RT   of the lyase from a huge precursor protein in Bacillus sp. GL1.";
RL   Arch. Biochem. Biophys. 354:31-39(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 36-41; 1169-1194 AND 1203-1205, FUNCTION, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PROTEOLYTIC PROCESSING.
RC   STRAIN=GL1;
RX   PubMed=14759609; DOI=10.1016/j.abb.2003.12.015;
RA   Miyake O., Kobayashi E., Nankai H., Hashimoto W., Mikami B., Murata K.;
RT   "Posttranslational processing of polysaccharide lyase: maturation route for
RT   gellan lyase in Bacillus sp. GL1.";
RL   Arch. Biochem. Biophys. 422:211-220(2004).
RN   [3]
RP   CATALYTIC ACTIVITY.
RC   STRAIN=GL1;
RX   PubMed=9056228; DOI=10.1006/abbi.1996.9851;
RA   Hashimoto W., Maesaka K., Sato N., Kimura S., Yamamoto K., Kumagai H.,
RA   Murata K.;
RT   "Microbial system for polysaccharide depolymerization: enzymatic route for
RT   gellan depolymerization by Bacillus sp. GL1.";
RL   Arch. Biochem. Biophys. 339:17-23(1997).
CC   -!- FUNCTION: Cleaves the glycosidic bonds of gellan backbone and releases
CC       tetrasaccharide units of glucuronyl-glucosyl-rhamnosyl-glucose with
CC       unsaturated glucuronic acid at the non-reducing terminal. The enzyme is
CC       highly specific to the heteropolysaccharide gellan, especially
CC       deacetylated gellan. {ECO:0000269|PubMed:14759609,
CC       ECO:0000269|PubMed:9633595}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Eliminative cleavage of beta-D-glucopyranosyl-(1->4)-beta-D-
CC         glucopyranosyluronate bonds of gellan backbone releasing
CC         tetrasaccharides containing a 4-deoxy-4,5-unsaturated D-
CC         glucopyranosyluronic acid at the non-reducing end. The
CC         tetrasaccharide produced from deacetylated gellan is beta-D-4-deoxy-
CC         Delta(4)-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-
CC         Glcp.; EC=4.2.2.25; Evidence={ECO:0000269|PubMed:14759609,
CC         ECO:0000269|PubMed:9056228, ECO:0000269|PubMed:9633595};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 6.0 in potassium phosphate and 7.5 in HEPES buffer.
CC         {ECO:0000269|PubMed:14759609};
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- PTM: Subject to proteolytic processing after secretion. Cleavage occurs
CC       between Gly-1205 and Leu-1206. This gives rise to a N-terminal gellan
CC       lyase of 130 kDa being the mature form of the gellan lyase. The
CC       function of C-terminal gellan lyase is not known.
CC       {ECO:0000269|PubMed:14759609}.
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DR   EMBL; AB006853; BAA29068.1; -; Genomic_DNA.
DR   PIR; T00047; T00047.
DR   AlphaFoldDB; O82833; -.
DR   KEGG; ag:BAA29068; -.
DR   BioCyc; MetaCyc:MON-16405; -.
DR   BRENDA; 4.2.2.25; 691.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR   GO; GO:0052762; F:gellan lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:InterPro.
DR   CDD; cd00063; FN3; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR002102; Cohesin_dom.
DR   InterPro; IPR003961; FN3_dom.
DR   InterPro; IPR036116; FN3_sf.
DR   InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002509; NODB_dom.
DR   Pfam; PF00963; Cohesin; 1.
DR   Pfam; PF01522; Polysacc_deac_1; 1.
DR   SMART; SM00060; FN3; 1.
DR   SUPFAM; SSF49265; SSF49265; 1.
DR   SUPFAM; SSF88713; SSF88713; 1.
DR   PROSITE; PS50853; FN3; 1.
DR   PROSITE; PS51677; NODB; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Lyase; Secreted; Signal.
FT   SIGNAL          1..35
FT                   /evidence="ECO:0000269|PubMed:14759609,
FT                   ECO:0000269|PubMed:9633595"
FT   CHAIN           36..2475
FT                   /note="Gellan lyase"
FT                   /id="PRO_0000424089"
FT   CHAIN           36..1205
FT                   /note="N-terminal gellan lyase"
FT                   /id="PRO_0000424090"
FT   CHAIN           1206..2475
FT                   /note="C-terminal gellan lyase"
FT                   /id="PRO_0000424091"
FT   DOMAIN          623..708
FT                   /note="Fibronectin type-III"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT   DOMAIN          1295..1518
FT                   /note="NodB homology"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01014"
FT   DOMAIN          2111..2223
FT                   /note="Cohesin"
FT   SITE            1205..1206
FT                   /note="Cleavage"
SQ   SEQUENCE   2475 AA;  263045 MW;  0184ED2F01CAFDF2 CRC64;
     MRFSWKKLVS AALVMALLVG IVYPAASGRG AVASAASGTT VELVPTDDAF TSAVAKDANA
     NGTWMQLKGS IGGQRYIYMK FDLTALAGVE ADRIENAKVW LKKMGTNGTA MTVGLRAVDD
     TSWSESTLTW NNAPVYGSQV LSQQSVLSTP DVYYPFDLDE YLKTQLAAGK SKLAIAFVPI
     STLNENMEFY ARESTANTPK LVVELKDEPP APTGLMQLVQ SFGGHNKGHL RVVEFDATPA
     STTGNGTVGI TADGAAPAAA ADFPIALRFG TDGTIKAANA AGFESKTPVN YTAGQKYHVK
     AMINLSLGTY DLWLTPPNAG QPVLLAADYA FAASAPALND IGGVHATADA QSTDVPAVAN
     ARLIADHFVS KAPFKDEQGQ SLAIRLESDN SLANRSYAIK FDMNLTGNPL ETDALISYAD
     RSVTLNGFPD LAYIVRSNFG NFDVRNDNVY ASSHPSTAQS NRTYQVEVRI NPASGTGQPT
     RTYDVWIAPE GEQPVQLADQ FKARNYANTG YALNNIGQAF VYSQADGLLS IDNHVVQDGQ
     RLDEALARVN AASGEAAMTA ALESNALGLP MERYRLMDAA KRAQVAQDVL AGRPAEGYAH
     ALSVQAVFVS AVANRLDTEN PTAPANVQVA ISNTMQAHVS WTASSDDTGI LYYKVFRDGA
     LVGTVTNATS FVDNGLAPAT EYTYVVKAYD LVLKEAVSQP ATATSPGEQA QVRIPFSAEA
     IATAFGQPLL DYNLETHSGT LKWVMEWREE YEKSANALKL LTLLSASAPD YIGPDGVTTA
     SAKALQHLRS VTAGGNEPGF AGNGLSGQGY MPLLSAIVMA KKKAPAIWNA LTAAEKEKLD
     LMILAGLYGA KFAYDDENDN KTGIDATGNF DKEWNPNHRS GIAGAIMAMY YFEDAQWLND
     QMRSFNYDDW LARLTAAGLT NVRTIYQNSG KTLTEREIRK DAAGDGFVYK GHPLSQPGKI
     MAEFVNYTFS HPVSPVGGFD SGIGKYRGYI VDGQDDLPNL GADSMGFEFD TLDANGKRSS
     LVYVFMGWKP NVDAITPVLL LDNIDSGLTS AETRDVVSRL SIGTTDMLYK NEHGYMTYAK
     GVNEGVKSLN GPILTINEEI WNRILNNPAA PMEAVNQASS AGQMRTALEA SALGMILYGY
     GALSETGKNA VAQHVLDARP AAGYANKAAA QNELYEGVRL QALLALSQAQ TAEQMRSALE
     SRALGLYKPK YETASQDKKQ FVAQYLLDNK PADGFLTKTE VREQVESALE PQGNQLRNLP
     PLASGEKRIN LADYDHWPQQ HGDAEVALWA DDKTGAFSLT IDDNFENEHD TWRSLAQQYG
     FKFSWFVITS LIKDPNKWRT LAAEGHEIGS HTVTHEDKGS TLDPAHLHSE YADSQALLNT
     IEGVRATTLA YPFGSGREDI AAEYYIAARG TVGLPNPADS INYMNTQSLS VRPGSLELTN
     QAANGNSVEA MVKTLVDPNH KVWSASYYRG WSNMLVHSLN ESGKTPSDGV TRTSRDLTQY
     LLTLLDTYRD QIWVGRYGDI VRYSQQRDTA HIVVTRKDDR KITFNLTDRM DDTLFDYPLT
     VKVRVDDAWS DIGATQAGEP IPFVETIRDG KRYLLVKAVP DKGSVSIVPD AASPLNVVNG
     AVTSEQMLSA IAAPGLGLDL GEFNALGAGK KRMVGSRLLE VRPADGYADA AALQDALDAA
     VEEANNAPSL SENASLSDLK VNGVTIAGFA PETYAYDIML PEGTTALPVV SFKVADTGKA
     TAVLQNAPAL PGTAKVTVTA EDNWTVATYT LRFQVRISAL QRVNTAPDAS AMRTAIENAA
     LGLVLAAYNG LTSEQKNSVA ASVLTHRPAT GYADVQAVQA ELNAALPKIN APLLAHAIVD
     QLNPDTVSTA NWTNLYGGTS GRKGGVYMKF NIASLAGLEA DAIGDAKVQF FTTREGTVIG
     YAAPSSWEAP LTWNTQPLAD LKNSNMAALA EIGRTAVQAT GANYEMNITQ YVKDAAAADK
     TELSLVLLGS NNTNITMQKI PTAFALSVTL ATYGEPNPEP SPLAAVNEAG DAAAMQGAIA
     AVELDLNLTA YNGLTAAQRI DVAQALLDNR PAAGYAHALA VQVALDAAVA AAQPANQAPG
     GTLAASAEQL QPGQQLELTV GVSDASRFTG ADILVHYDPQ ALTFATELYE GVRMLKAEAI
     ASLQANYQVA AAMAEQPGTI KILLFTAGAG QPLSGTLPLF KLRASVKDDA QTGVSTAVSL
     SDFELTFEGE DSVWPDTTRA AVSLQIAAHP VEADKTALIA KIAHAQALLT GATVGANPGQ
     YPQAAYDALA DAIGLAEEKR DLTGVSQAAV DEAVASLGTA EQQFLNAVIP GVPADLTALN
     AAIAKAQRLH DNGPYGEKIG QYPQSAKVPL KSALDAAKAV GGSGASSQES VNAAAASLNG
     AIQTFERSLV TLVGGGATKV GIRDLSIVAK YYGVTSSDPN WGKVSAAAID GGNEITIEVL
     AAVARMILAD WAAGQ