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Q54873

- HYSA_STRPN

UniProt

Q54873 - HYSA_STRPN

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Protein
Hyaluronate lyase
Gene
SP_0314
Organism
Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

Functioni

Catalytic activityi

Cleaves hyaluronate chains at a beta-D-GalNAc-(1->4)-beta-D-GlcA bond, ultimately breaking the polysaccharide down to 3-(4-deoxy-beta-D-gluc-4-enuronosyl)-N-acetyl-D-glucosamine.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei466 – 4661
Active sitei516 – 5161
Active sitei525 – 5251

GO - Molecular functioni

  1. carbohydrate binding Source: InterPro
  2. hyaluronate lyase activity Source: UniProtKB-EC

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciSPNE170187:GHGN-320-MONOMER.
BRENDAi4.2.2.1. 5946.
SABIO-RKQ54873.

Protein family/group databases

CAZyiPL8. Polysaccharide Lyase Family 8.

Names & Taxonomyi

Protein namesi
Recommended name:
Hyaluronate lyase (EC:4.2.2.1)
Alternative name(s):
Hyaluronidase
Short name:
HYase
Gene namesi
Ordered Locus Names:SP_0314
OrganismiStreptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4)
Taxonomic identifieri170187 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000585: Chromosome

Subcellular locationi

Secretedcell wall; Peptidoglycan-anchor Reviewed prediction

GO - Cellular componenti

  1. cell wall Source: UniProtKB-SubCell
  2. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi360 – 3601R → V: Retains 67% of wild-type activity. 1 Publication
Mutagenesisi466 – 4661N → A: Almost complete loss of activity. 1 Publication
Mutagenesisi516 – 5161H → A: Almost complete loss of activity. 1 Publication
Mutagenesisi525 – 5251Y → F: Complete loss of activity. 1 Publication
Mutagenesisi697 – 6971N → G: Slightly increased activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3030 Reviewed prediction
Add
BLAST
Chaini31 – 10391009Hyaluronate lyase
PRO_0000024933Add
BLAST
Propeptidei1040 – 106627Removed by sortase Reviewed prediction
PRO_0000024934Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1039 – 10391Pentaglycyl murein peptidoglycan amidated threonine Reviewed prediction

Keywords - PTMi

Peptidoglycan-anchor

Proteomic databases

PRIDEiQ54873.

Interactioni

Protein-protein interaction databases

STRINGi170187.SP_0314.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi290 – 30213
Helixi305 – 3073
Beta strandi310 – 3123
Helixi313 – 33220
Beta strandi336 – 3383
Beta strandi340 – 3423
Helixi344 – 3463
Beta strandi349 – 3513
Helixi353 – 36917
Turni375 – 3784
Helixi380 – 39617
Beta strandi398 – 4014
Helixi408 – 4125
Helixi414 – 42512
Helixi427 – 4293
Helixi432 – 44514
Beta strandi451 – 4533
Beta strandi456 – 4583
Helixi464 – 48017
Helixi484 – 49411
Helixi495 – 4984
Beta strandi502 – 5076
Beta strandi513 – 5153
Turni516 – 5183
Turni522 – 5243
Helixi525 – 54016
Beta strandi543 – 5453
Helixi549 – 5524
Helixi554 – 5618
Helixi564 – 5663
Helixi574 – 5763
Helixi578 – 5825
Helixi584 – 5863
Helixi588 – 60518
Helixi608 – 62417
Beta strandi626 – 6283
Helixi630 – 6334
Helixi637 – 64812
Beta strandi660 – 6645
Helixi665 – 6673
Beta strandi669 – 6746
Turni675 – 6784
Beta strandi679 – 6846
Beta strandi690 – 6923
Turni704 – 7074
Beta strandi711 – 7144
Turni718 – 7214
Helixi725 – 7284
Helixi731 – 7333
Beta strandi738 – 7403
Beta strandi758 – 7603
Beta strandi767 – 7759
Beta strandi779 – 78911
Beta strandi794 – 80310
Beta strandi805 – 8073
Beta strandi809 – 8179
Beta strandi820 – 8223
Beta strandi825 – 8284
Beta strandi831 – 8333
Beta strandi840 – 85112
Helixi855 – 8573
Beta strandi859 – 87820
Helixi880 – 8823
Beta strandi892 – 90211
Beta strandi908 – 91710
Helixi920 – 92910
Turni930 – 9323
Beta strandi934 – 94613
Turni947 – 9504
Beta strandi951 – 9588
Beta strandi962 – 9643
Turni965 – 9673
Beta strandi968 – 9703
Beta strandi972 – 98110
Beta strandi984 – 9918
Turni992 – 9954
Helixi1000 – 10034
Beta strandi1004 – 10063

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C82X-ray1.70A285-1009[»]
1EGUX-ray1.56A285-1009[»]
1F9GX-ray2.00A285-1009[»]
1LOHX-ray2.00A287-1007[»]
1LXKX-ray1.53A287-1007[»]
1N7NX-ray1.55A287-1007[»]
1N7OX-ray1.50A287-1007[»]
1N7PX-ray1.55A287-1007[»]
1N7QX-ray2.30A287-1007[»]
1N7RX-ray2.20A287-1007[»]
1OJMX-ray1.78A291-1009[»]
1OJNX-ray1.60A285-1009[»]
1OJOX-ray1.75A285-1009[»]
1OJPX-ray1.90A285-1009[»]
1W3YX-ray1.65A285-1009[»]
2BRPX-ray2.00A285-1009[»]
2BRVX-ray3.30X285-1009[»]
2BRWX-ray2.80A/B285-1009[»]
ProteinModelPortaliQ54873.
SMRiQ54873. Positions 212-1008.

Miscellaneous databases

EvolutionaryTraceiQ54873.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1036 – 10405LPXTG sorting signal Reviewed prediction

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG04835.
HOGENOMiHOG000008667.
KOiK01727.
OMAiRYYQDET.
OrthoDBiEOG6GBM67.

Family and domain databases

Gene3Di1.50.10.100. 1 hit.
2.60.120.260. 1 hit.
2.60.220.10. 1 hit.
2.60.40.1380. 1 hit.
2.70.98.10. 1 hit.
InterProiIPR008929. Chondroitin_lyas.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR023295. Hyaluronate_lyase_beta_dom.
IPR014756. Ig_E-set.
IPR019931. LPXTG_anchor.
IPR011071. Lyase_8-like_C.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
[Graphical view]
PfamiPF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF08124. Lyase_8_N. 1 hit.
[Graphical view]
SUPFAMiSSF48230. SSF48230. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF49863. SSF49863. 1 hit.
SSF74650. SSF74650. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsiTIGR01167. LPXTG_anchor. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q54873-1 [UniParc]FASTAAdd to Basket

« Hide

MQTKTKKLIV SLSSLVLSGF LLNHYMTIGA EETTTNTIQQ SQKEVQYQQR     50
DTKNLVENGD FGQTEDGSSP WTGSKAQGWS AWVDQKNSAD ASTRVIEAKD 100
GAITISSHEK LRAALHRMVP IEAKKKYKLR FKIKTDNKIG IAKVRIIEES 150
GKDKRLWNSA TTSGTKDWQT IEADYSPTLD VDKIKLELFY ETGTGTVSFK 200
DIELVEVADQ LSEDSQTDKQ LEEKIDLPIG KKHVFSLADY TYKVENPDVA 250
SVKNGILEPL KEGTTNVIVS KDGKEVKKIP LKILASVKDA YTDRLDDWNG 300
IIAGNQYYDS KNEQMAKLNQ ELEGKVADSL SSISSQADRT YLWEKFSNYK 350
TSANLTATYR KLEEMAKQVT NPSSRYYQDE TVVRTVRDSM EWMHKHVYNS 400
EKSIVGNWWD YEIGTPRAIN NTLSLMKEYF SDEEIKKYTD VIEKFVPDPE 450
HFRKTTDNPF KALGGNLVDM GRVKVIAGLL RKDDQEISST IRSIEQVFKL 500
VDQGEGFYQD GSYIDHTNVA YTGAYGNVLI DGLSQLLPVI QKTKNPIDKD 550
KMQTMYHWID KSFAPLLVNG ELMDMSRGRS ISRANSEGHV AAVEVLRGIH 600
RIADMSEGET KQCLQSLVKT IVQSDSYYDV FKNLKTYKDI SLMQSLLSDA 650
GVASVPRPSY LSAFNKMDKT AMYNAEKGFG FGLSLFSSRT LNYEHMNKEN 700
KRGWYTSDGM FYLYNGDLSH YSDGYWPTVN PYKMPGTTET DAKRADSDTG 750
KVLPSAFVGT SKLDDANATA TMDFTNWNQT LTAHKSWFML KDKIAFLGSN 800
IQNTSTDTAA TTIDQRKLES GNPYKVYVND KEASLTEQEK DYPETQSVFL 850
ESFDSKKNIG YFFFKKSSIS MSKALQKGAW KDINEGQSDK EVENEFLTIS 900
QAHKQNRDSY GYMLIPNVDR ATFNQMIKEL ESSLIENNET LQSVYDAKQG 950
VWGIVKYDDS VSTISNQFQV LKRGVYTIRK EGDEYKIAYY NPETQESAPD 1000
QEVFKKLEQA AQPQVQNSKE KEKSEEEKNH SDQKNLPQTG EGQSILASLG 1050
FLLLGAFYLF RRGKNN 1066
Length:1,066
Mass (Da):120,771
Last modified:September 26, 2001 - v2
Checksum:i81DB22A837BE61F9
GO

Sequence cautioni

The sequence AAA53685.1 differs from that shown. Reason: Erroneous initiation.
The sequence AAA53686.1 differs from that shown. Reason: Erroneous initiation.

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081H → P1 Publication
Sequence conflicti115 – 1151L → V1 Publication
Sequence conflicti139 – 1391I → V in AAA53685. 1 Publication
Sequence conflicti211 – 2111L → P in AAA53685. 1 Publication
Sequence conflicti236 – 2361S → P in AAA53685. 1 Publication
Sequence conflicti290 – 2901A → T in AAA53685. 1 Publication
Sequence conflicti290 – 2901A → T in AAA53686. 1 Publication
Sequence conflicti313 – 3131E → D in AAA53685. 1 Publication
Sequence conflicti313 – 3131E → D in AAA53686. 1 Publication
Sequence conflicti340 – 3401T → I in AAA53685. 1 Publication
Sequence conflicti340 – 3401T → I in AAA53686. 1 Publication
Sequence conflicti613 – 6131C → R in AAA53685. 1 Publication
Sequence conflicti613 – 6131C → R in AAA53686. 1 Publication
Sequence conflicti658 – 6581P → T in AAA53685. 1 Publication
Sequence conflicti658 – 6581P → T in AAA53686. 1 Publication
Sequence conflicti821 – 8211G → S in AAA53685. 1 Publication
Sequence conflicti821 – 8211G → S in AAA53686. 1 Publication
Sequence conflicti848 – 8481V → G in AAA53685. 1 Publication
Sequence conflicti848 – 8481V → G in AAA53686. 1 Publication
Sequence conflicti853 – 8531F → S in AAA53685. 1 Publication
Sequence conflicti853 – 8531F → S in AAA53686. 1 Publication
Sequence conflicti907 – 9071R → G in AAA53685. 1 Publication
Sequence conflicti907 – 9071R → G in AAA53686. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005672 Genomic DNA. Translation: AAK74491.1.
L20670 Genomic DNA. Translation: AAA53685.1. Different initiation.
L20670 Genomic DNA. Translation: AAA53686.1. Different initiation.
PIRiB95037.
RefSeqiNP_344851.1. NC_003028.3.
WP_001193686.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK74491; AAK74491; SP_0314.
GeneIDi930127.
KEGGispn:SP_0314.
PATRICi19704965. VBIStrPne105772_0328.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005672 Genomic DNA. Translation: AAK74491.1 .
L20670 Genomic DNA. Translation: AAA53685.1 . Different initiation.
L20670 Genomic DNA. Translation: AAA53686.1 . Different initiation.
PIRi B95037.
RefSeqi NP_344851.1. NC_003028.3.
WP_001193686.1. NZ_AKVY01000001.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1C82 X-ray 1.70 A 285-1009 [» ]
1EGU X-ray 1.56 A 285-1009 [» ]
1F9G X-ray 2.00 A 285-1009 [» ]
1LOH X-ray 2.00 A 287-1007 [» ]
1LXK X-ray 1.53 A 287-1007 [» ]
1N7N X-ray 1.55 A 287-1007 [» ]
1N7O X-ray 1.50 A 287-1007 [» ]
1N7P X-ray 1.55 A 287-1007 [» ]
1N7Q X-ray 2.30 A 287-1007 [» ]
1N7R X-ray 2.20 A 287-1007 [» ]
1OJM X-ray 1.78 A 291-1009 [» ]
1OJN X-ray 1.60 A 285-1009 [» ]
1OJO X-ray 1.75 A 285-1009 [» ]
1OJP X-ray 1.90 A 285-1009 [» ]
1W3Y X-ray 1.65 A 285-1009 [» ]
2BRP X-ray 2.00 A 285-1009 [» ]
2BRV X-ray 3.30 X 285-1009 [» ]
2BRW X-ray 2.80 A/B 285-1009 [» ]
ProteinModelPortali Q54873.
SMRi Q54873. Positions 212-1008.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 170187.SP_0314.

Chemistry

BindingDBi Q54873.
ChEMBLi CHEMBL1795158.
DrugBanki DB00126. Vitamin C.

Protein family/group databases

CAZyi PL8. Polysaccharide Lyase Family 8.

Proteomic databases

PRIDEi Q54873.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAK74491 ; AAK74491 ; SP_0314 .
GeneIDi 930127.
KEGGi spn:SP_0314.
PATRICi 19704965. VBIStrPne105772_0328.

Phylogenomic databases

eggNOGi NOG04835.
HOGENOMi HOG000008667.
KOi K01727.
OMAi RYYQDET.
OrthoDBi EOG6GBM67.

Enzyme and pathway databases

BioCyci SPNE170187:GHGN-320-MONOMER.
BRENDAi 4.2.2.1. 5946.
SABIO-RK Q54873.

Miscellaneous databases

EvolutionaryTracei Q54873.

Family and domain databases

Gene3Di 1.50.10.100. 1 hit.
2.60.120.260. 1 hit.
2.60.220.10. 1 hit.
2.60.40.1380. 1 hit.
2.70.98.10. 1 hit.
InterProi IPR008929. Chondroitin_lyas.
IPR011013. Gal_mutarotase_SF_dom.
IPR008979. Galactose-bd-like.
IPR014718. Glyco_hydro-type_carb-bd_sub.
IPR023295. Hyaluronate_lyase_beta_dom.
IPR014756. Ig_E-set.
IPR019931. LPXTG_anchor.
IPR011071. Lyase_8-like_C.
IPR012970. Lyase_8_alpha_N.
IPR004103. Lyase_8_C.
IPR003159. Lyase_8_central_dom.
IPR012329. Lyase_8_N.
[Graphical view ]
Pfami PF02278. Lyase_8. 1 hit.
PF02884. Lyase_8_C. 1 hit.
PF08124. Lyase_8_N. 1 hit.
[Graphical view ]
SUPFAMi SSF48230. SSF48230. 1 hit.
SSF49785. SSF49785. 1 hit.
SSF49863. SSF49863. 1 hit.
SSF74650. SSF74650. 1 hit.
SSF81296. SSF81296. 1 hit.
TIGRFAMsi TIGR01167. LPXTG_anchor. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-334 / TIGR4.
  2. "Cloning and nucleotide sequence of the Streptococcus pneumoniae hyaluronidase gene and purification of the enzyme from recombinant Escherichia coli."
    Berry A.M., Lock R.A., Thomas S.M., Rajan D.P., Hansman D., Paton J.C.
    Infect. Immun. 62:1101-1108(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 89-1066.
    Strain: Type 23.
  3. "Crystallization and preliminary X-ray analysis of Streptococcus pneumoniae hyaluronate lyase."
    Jedrzejas M.J., Chantalat L., Mewbourne R.B.
    J. Struct. Biol. 121:73-75(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
  4. "Structural basis of hyaluronan degradation by Streptococcus pneumoniae hyaluronate lyase."
    Li S., Kelly S.J., Lamani E., Ferraroni M., Jedrzejas M.J.
    EMBO J. 19:1228-1240(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 285-1015, MUTAGENESIS OF ARG-360; ASN-466; HIS-516; TYR-525 AND ASN-697.

Entry informationi

Entry nameiHYSA_STRPN
AccessioniPrimary (citable) accession number: Q54873
Secondary accession number(s): Q54874
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: September 26, 2001
Last modified: September 3, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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