HYSA_STRA3
ID HYSA_STRA3 Reviewed; 984 AA.
AC Q53591;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 17-JAN-2003, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Hyaluronate lyase {ECO:0000303|PubMed:7982914};
DE EC=4.2.2.1 {ECO:0000269|PubMed:7982914};
DE AltName: Full=Hyaluronidase;
DE Short=HYase;
DE Flags: Precursor;
GN Name=hylB {ECO:0000303|PubMed:7982914}; OrderedLocusNames=gbs1270;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RC STRAIN=3502 / Serotype III;
RX PubMed=7982914; DOI=10.1016/s0021-9258(18)43783-0;
RA Lin B., Hollingshead S.K., Coligan J.E., Egan M.L., Baker J.R.,
RA Pritchard D.G.;
RT "Cloning and expression of the gene for group B streptococcal hyaluronate
RT lyase.";
RL J. Biol. Chem. 269:30113-30116(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 171-984, AND ACTIVE SITE.
RX PubMed=11527972; DOI=10.1074/jbc.m106634200;
RA Li S., Jedrzejas M.J.;
RT "Hyaluronan binding and degradation by Streptococcus agalactiae hyaluronate
RT lyase.";
RL J. Biol. Chem. 276:41407-41416(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[hyaluronan](n) = n 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-
CC acetyl-D-glucosamine + H2O; Xref=Rhea:RHEA:50240, Rhea:RHEA-
CC COMP:12583, ChEBI:CHEBI:15377, ChEBI:CHEBI:132151,
CC ChEBI:CHEBI:132153; EC=4.2.2.1;
CC Evidence={ECO:0000269|PubMed:7982914};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the polysaccharide lyase 8 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAD46929.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U15050; AAA56749.1; -; Genomic_DNA.
DR EMBL; AL766849; CAD46929.1; ALT_INIT; Genomic_DNA.
DR PIR; A55137; A55137.
DR PDB; 1F1S; X-ray; 2.10 A; A=171-984.
DR PDB; 1I8Q; X-ray; 2.20 A; A=171-984.
DR PDB; 1LXM; X-ray; 2.20 A; A=171-984.
DR PDBsum; 1F1S; -.
DR PDBsum; 1I8Q; -.
DR PDBsum; 1LXM; -.
DR AlphaFoldDB; Q53591; -.
DR SMR; Q53591; -.
DR STRING; 211110.gbs1270; -.
DR DrugBank; DB04548; 4-Deoxy-D-Glucuronic Acid.
DR CAZy; CBM70; Carbohydrate-Binding Module Family 70.
DR CAZy; PL8; Polysaccharide Lyase Family 8.
DR EnsemblBacteria; CAD46929; CAD46929; CAD46929.
DR KEGG; san:gbs1270; -.
DR eggNOG; COG5492; Bacteria.
DR HOGENOM; CLU_004172_0_0_9; -.
DR BRENDA; 4.2.2.1; 5917.
DR EvolutionaryTrace; Q53591; -.
DR PHI-base; PHI:3461; -.
DR Proteomes; UP000000823; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro.
DR GO; GO:0030340; F:hyaluronate lyase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR Gene3D; 1.50.10.100; -; 1.
DR Gene3D; 2.60.220.10; -; 1.
DR Gene3D; 2.60.40.1380; -; 1.
DR Gene3D; 2.70.98.10; -; 1.
DR InterPro; IPR008929; Chondroitin_lyas.
DR InterPro; IPR011013; Gal_mutarotase_sf_dom.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR InterPro; IPR014718; GH-type_carb-bd.
DR InterPro; IPR023295; Hyaluronate_lyase_beta_dom_sf.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR038970; Lyase_8.
DR InterPro; IPR011071; Lyase_8-like_C.
DR InterPro; IPR012970; Lyase_8_alpha_N.
DR InterPro; IPR004103; Lyase_8_C.
DR InterPro; IPR003159; Lyase_8_central_dom.
DR PANTHER; PTHR38481; PTHR38481; 1.
DR Pfam; PF02278; Lyase_8; 1.
DR Pfam; PF02884; Lyase_8_C; 1.
DR Pfam; PF08124; Lyase_8_N; 1.
DR SUPFAM; SSF48230; SSF48230; 1.
DR SUPFAM; SSF49785; SSF49785; 1.
DR SUPFAM; SSF49863; SSF49863; 1.
DR SUPFAM; SSF74650; SSF74650; 1.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Lyase; Secreted; Signal.
FT SIGNAL 1..40
FT /evidence="ECO:0000255"
FT CHAIN 41..984
FT /note="Hyaluronate lyase"
FT /id="PRO_0000024932"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 49..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 701..728
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 52..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 701..727
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 429
FT /evidence="ECO:0000305|PubMed:11527972"
FT ACT_SITE 479
FT /evidence="ECO:0000305|PubMed:11527972"
FT ACT_SITE 488
FT /evidence="ECO:0000305|PubMed:11527972"
FT CONFLICT 45
FT /note="E -> G (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 155..156
FT /note="SA -> FV (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 183
FT /note="E -> K (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 246..251
FT /note="ASTEDK -> GSPEDN (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 267
FT /note="H -> Y (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 279..280
FT /note="IN -> LT (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 288
FT /note="A -> G (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 292..293
FT /note="KT -> EA (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="H -> R (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 384
FT /note="A -> G (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 387
FT /note="A -> S (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 413
FT /note="G -> E (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 420
FT /note="D -> V (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 583
FT /note="T -> A (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 609
FT /note="M -> L (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 639
FT /note="E -> K (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 666
FT /note="D -> G (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 676
FT /note="L -> I (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 688..689
FT /note="FW -> LG (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 882
FT /note="Q -> L (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="M -> L (in Ref. 1; AAA56749)"
FT /evidence="ECO:0000305"
FT STRAND 185..188
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 196..199
FT /evidence="ECO:0007829|PDB:1LXM"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 207..209
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 210..213
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 216..219
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 223..230
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 236..245
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 251..263
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 274..293
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 305..307
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 313..330
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 336..339
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 341..357
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:1LXM"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 377..388
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 395..408
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 414..416
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 417..420
FT /evidence="ECO:0007829|PDB:1I8Q"
FT HELIX 427..443
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 447..457
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 458..460
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 464..471
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 476..478
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 479..481
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 485..487
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 488..503
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 512..524
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 527..529
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 537..539
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 541..545
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 551..566
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 572..587
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 589..591
FT /evidence="ECO:0007829|PDB:1LXM"
FT HELIX 593..596
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 600..611
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 628..630
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 632..637
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 638..641
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 642..647
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 653..655
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:1LXM"
FT TURN 667..670
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 671..677
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 681..684
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 685..687
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 688..691
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 694..696
FT /evidence="ECO:0007829|PDB:1I8Q"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 712..716
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 717..720
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 722..726
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 736..753
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 757..768
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 771..781
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 782..784
FT /evidence="ECO:0007829|PDB:1I8Q"
FT STRAND 788..796
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 799..801
FT /evidence="ECO:0007829|PDB:1I8Q"
FT STRAND 804..807
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 816..831
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 839..858
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 860..863
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 873..883
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 886..888
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 891..898
FT /evidence="ECO:0007829|PDB:1F1S"
FT HELIX 901..909
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 912..918
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 920..927
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 928..931
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 932..937
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 943..945
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 946..948
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 949..951
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 955..962
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 965..972
FT /evidence="ECO:0007829|PDB:1F1S"
FT TURN 973..976
FT /evidence="ECO:0007829|PDB:1F1S"
FT STRAND 977..981
FT /evidence="ECO:0007829|PDB:1F1S"
SQ SEQUENCE 984 AA; 111581 MW; AC7215ED6D5C2592 CRC64;
MKQVVDNQTQ NKELVKNGDF NQTNPVSGSW SHTSAREWSA WIDKENTADK SPIIQRTEQG
QVSLSSDKGF RGAVTQKVNI DPTKKYEVKF DIETSNKAGQ AFLRIMEKKD NNTRLWLSEM
TSGTTNKHTL TKIYNPKLNV SEVTLELYYE KGTGSATFDN ISMKAKGPKD SEHPQPVTTQ
IEESVNTALN KNYVFNKADY QYTLTNPSLG KIVGGILYPN ATGSTTVKIS DKSGKIIKEV
PLSVTASTED KFTKLLDKWN DVTIGNHVYD TNDSNMQKIN QKLDETNAKN IKTIKLDSNH
TFLWKDLDNL NNSAQLTATY RRLEDLAKQI TNPHSTIYKN EKAIRTVKES LAWLHQNFYN
VNKDIEGSAN WWDFEIGVPR SITATLALMN NYFTDAEIKT YTDPIEHFVP DAGYFRKTLD
NPFKALGGNL VDMGRVKIIE GLLRKDNTII EKTSHSLKNL FTTATKAEGF YADGSYIDHT
NVAYTGAYGN VLIDGLTQLL PIIQETDYKI SNQELDMVYK WINQSFLPLI VKGELMDMSR
GRSISREAAS SHAAAVEVLR GFLRLANMSN EERNLDLKST IKTIITSNKF YNVFNNLKSY
SDIANMNKML NDSTVATKPL KSNLSTFNSM DRLAYYNAEK DFGFALSLHS KRTLNYEGMN
DENTRDWYTG DGMFYLYNSD QSHYSNHFWP TVNPYKMAGT TEKDAKREDT TKEFMSKHSK
DAKEKTGQVT GTSDFVGSVK LNDHFALAAM DFTNWDRTLT AQKGWVILND KIVFLGSNIK
NTNGIGNVST TIDQRKDDSK TPYTTYVNGK TIDLKQASSQ QFTDTKSVFL ESKEPGRNIG
YIFFKNSTID IERKEQTGTW NSINRTSKNT SIVSNPFITI SQKHDNKGDS YGYMMVPNID
RTSFDKLANS KEVELLENSS KQQVIYDKNS QTWAVIKHDN QESLINNQFK MNKAGLYLVQ
KVGNDYQNVY YQPQTMTKTD QLAI
