HYLP1_BPH44
ID HYLP1_BPH44 Reviewed; 371 AA.
AC P15316;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 25-MAY-2022, entry version 69.
DE RecName: Full=Hyaluronoglucosaminidase;
DE Short=Hyaluronidase;
DE EC=3.2.1.35;
GN Name=HYLP1; Synonyms=HYLP;
OS Streptococcus pyogenes phage H4489A.
OC Viruses; unclassified bacterial viruses.
OX NCBI_TaxID=12366;
OH NCBI_TaxID=1314; Streptococcus pyogenes.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2643574; DOI=10.1128/iai.57.2.533-539.1989;
RA Hynes W.L., Ferretti J.J.;
RT "Sequence analysis and expression in Escherichia coli of the hyaluronidase
RT gene of Streptococcus pyogenes bacteriophage H4489A.";
RL Infect. Immun. 57:533-539(1989).
CC -!- FUNCTION: The hyaluronidase of this bacteriophage mediates the
CC penetration of the hyaluronic capsule of Streptococcus pyogenes.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-
CC glucosamine and D-glucuronate residues in hyaluronate.; EC=3.2.1.35;
CC -!- SUBCELLULAR LOCATION: Virion {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 69 family. {ECO:0000305}.
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DR EMBL; M19348; AAA98101.1; -; Genomic_DNA.
DR PIR; A30566; HUBPHA.
DR PDB; 6WV2; X-ray; 2.21 A; A/B/C=87-371.
DR PDB; 6WWX; X-ray; 2.20 A; A/B/C=87-371.
DR PDB; 6WXA; X-ray; 2.30 A; A/B/C=87-371.
DR PDB; 6X3M; X-ray; 3.58 A; A/B/C/D/E/F/G/H/I=1-371.
DR PDBsum; 6WV2; -.
DR PDBsum; 6WWX; -.
DR PDBsum; 6WXA; -.
DR PDBsum; 6X3M; -.
DR SMR; P15316; -.
DR CAZy; PL16; Polysaccharide Lyase Family 16.
DR BRENDA; 4.2.2.1; 7637.
DR GO; GO:0004415; F:hyalurononglucosaminidase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:InterPro.
DR GO; GO:0098996; P:disruption of host cell glycocalyx during viral entry; IEA:UniProtKB-KW.
DR InterPro; IPR009860; Hyaluronidase_bac.
DR InterPro; IPR041352; Mtd_N.
DR Pfam; PF07212; Hyaluronidase_1; 1.
DR Pfam; PF18454; Mtd_N; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Degradation of host capsule during virus entry;
KW Degradation of host cell envelope components during virus entry;
KW Glycosidase; Hydrolase; Virion; Virus entry into host cell.
FT CHAIN 1..371
FT /note="Hyaluronoglucosaminidase"
FT /id="PRO_0000057723"
FT REGION 54..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT HELIX 107..116
FT /evidence="ECO:0007829|PDB:6WWX"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:6WV2"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 148..150
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6WWX"
FT TURN 161..163
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 165..170
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 178..183
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 192..197
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 245..250
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 253..263
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 265..268
FT /evidence="ECO:0007829|PDB:6WWX"
FT TURN 269..274
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 276..283
FT /evidence="ECO:0007829|PDB:6WWX"
FT TURN 286..288
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 295..300
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 305..307
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:6WWX"
FT STRAND 334..338
FT /evidence="ECO:0007829|PDB:6WWX"
FT HELIX 354..371
FT /evidence="ECO:0007829|PDB:6WWX"
SQ SEQUENCE 371 AA; 39519 MW; 09D0DBC5F292B893 CRC64;
MTENIPLRVQ FKRMSADEWA RSDVILLEGE IGFETDTGFA KFGDGQNTFS KLKYLTGPKG
PKGDTGLQGK TGGTGPRGPA GKPGTTDYDQ LQNKPDLGAF AQKEETNSKI TKLESSKADK
SAVYSKAESK IELDKKLSLT GGIVTGQLQF KPNKSGIKPS SSVGGAINID MSKSEGAAMV
MYTNKDTTDG PLMILRSDKD TFDQSAQFVD YSGKTNAVNI VMRQPSAPNF SSALNITSAN
EGGSAMQIRG VEKALGTLKI THENPNVEAK YDENAAALSI DIVKKQKGGK GTAAQGIYIN
STSGTAGKML RIRNKNEDKF YVGPDGGFHS GANSTVAGNL TVKDPTSGKH AATKDYVDEK
IAELKKLILK K