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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

GO - Cellular componenti

  1. cell wall Source: UniProtKB-KW
  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 – 3030Sequence AnalysisAdd
BLAST
Chaini31 – 10391009Hyaluronate lyasePRO_0000024933Add
BLAST
Propeptidei1040 – 106627Removed by sortaseSequence AnalysisPRO_0000024934Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1039 – 10391Pentaglycyl murein peptidoglycan amidated threonineSequence Analysis

Keywords - PTMi

Peptidoglycan-anchor

Proteomic databases

PRIDEiQ54873.

Interactioni

Protein-protein interaction databases

STRINGi170187.SP_0314.

Structurei

Secondary structure

1
1066
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni57 – 604Combined sources
Beta strandi63 – 653Combined sources
Beta strandi80 – 834Combined sources
Helixi85 – 873Combined sources
Beta strandi95 – 995Combined sources
Beta strandi102 – 12019Combined sources
Beta strandi127 – 15024Combined sources
Beta strandi153 – 1586Combined sources
Beta strandi162 – 17514Combined sources
Beta strandi182 – 20625Combined sources
Helixi290 – 30213Combined sources
Helixi305 – 3073Combined sources
Beta strandi310 – 3123Combined sources
Helixi313 – 33220Combined sources
Beta strandi336 – 3383Combined sources
Beta strandi340 – 3423Combined sources
Helixi344 – 3463Combined sources
Beta strandi349 – 3513Combined sources
Helixi353 – 36917Combined sources
Turni375 – 3784Combined sources
Helixi380 – 39617Combined sources
Beta strandi398 – 4014Combined sources
Helixi408 – 4125Combined sources
Helixi414 – 42512Combined sources
Helixi427 – 4293Combined sources
Helixi432 – 44514Combined sources
Beta strandi451 – 4533Combined sources
Beta strandi456 – 4583Combined sources
Helixi464 – 48017Combined sources
Helixi484 – 49411Combined sources
Helixi495 – 4984Combined sources
Beta strandi502 – 5076Combined sources
Beta strandi513 – 5153Combined sources
Turni516 – 5183Combined sources
Turni522 – 5243Combined sources
Helixi525 – 54016Combined sources
Beta strandi543 – 5453Combined sources
Helixi549 – 5524Combined sources
Helixi554 – 5618Combined sources
Helixi564 – 5663Combined sources
Helixi574 – 5763Combined sources
Helixi578 – 5825Combined sources
Helixi584 – 5863Combined sources
Helixi588 – 60518Combined sources
Helixi608 – 62417Combined sources
Beta strandi626 – 6283Combined sources
Helixi630 – 6334Combined sources
Helixi637 – 64812Combined sources
Beta strandi660 – 6645Combined sources
Helixi665 – 6673Combined sources
Beta strandi669 – 6746Combined sources
Turni675 – 6784Combined sources
Beta strandi679 – 6846Combined sources
Beta strandi690 – 6923Combined sources
Turni704 – 7074Combined sources
Beta strandi711 – 7144Combined sources
Turni718 – 7214Combined sources
Helixi725 – 7284Combined sources
Helixi731 – 7333Combined sources
Beta strandi738 – 7403Combined sources
Beta strandi758 – 7603Combined sources
Beta strandi767 – 7759Combined sources
Beta strandi779 – 78911Combined sources
Beta strandi794 – 80310Combined sources
Beta strandi805 – 8073Combined sources
Beta strandi809 – 8179Combined sources
Beta strandi820 – 8223Combined sources
Beta strandi825 – 8284Combined sources
Beta strandi831 – 8333Combined sources
Beta strandi840 – 85112Combined sources
Helixi855 – 8573Combined sources
Beta strandi859 – 87820Combined sources
Helixi880 – 8823Combined sources
Beta strandi892 – 90211Combined sources
Beta strandi908 – 91710Combined sources
Helixi920 – 92910Combined sources
Turni930 – 9323Combined sources
Beta strandi934 – 94613Combined sources
Turni947 – 9504Combined sources
Beta strandi951 – 9588Combined sources
Beta strandi962 – 9643Combined sources
Turni965 – 9673Combined sources
Beta strandi968 – 9703Combined sources
Beta strandi972 – 98110Combined sources
Beta strandi984 – 9918Combined sources
Turni992 – 9954Combined sources
Helixi1000 – 10034Combined sources
Beta strandi1004 – 10063Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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[»]
4D0QX-ray1.20A54-212[»]
ProteinModelPortaliQ54873.
SMRiQ54873. Positions 212-1008.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ54873.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi1036 – 10405LPXTG sorting signalSequence Analysis

Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

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

        10         20         30         40         50
MQTKTKKLIV SLSSLVLSGF LLNHYMTIGA EETTTNTIQQ SQKEVQYQQR
60 70 80 90 100
DTKNLVENGD FGQTEDGSSP WTGSKAQGWS AWVDQKNSAD ASTRVIEAKD
110 120 130 140 150
GAITISSHEK LRAALHRMVP IEAKKKYKLR FKIKTDNKIG IAKVRIIEES
160 170 180 190 200
GKDKRLWNSA TTSGTKDWQT IEADYSPTLD VDKIKLELFY ETGTGTVSFK
210 220 230 240 250
DIELVEVADQ LSEDSQTDKQ LEEKIDLPIG KKHVFSLADY TYKVENPDVA
260 270 280 290 300
SVKNGILEPL KEGTTNVIVS KDGKEVKKIP LKILASVKDA YTDRLDDWNG
310 320 330 340 350
IIAGNQYYDS KNEQMAKLNQ ELEGKVADSL SSISSQADRT YLWEKFSNYK
360 370 380 390 400
TSANLTATYR KLEEMAKQVT NPSSRYYQDE TVVRTVRDSM EWMHKHVYNS
410 420 430 440 450
EKSIVGNWWD YEIGTPRAIN NTLSLMKEYF SDEEIKKYTD VIEKFVPDPE
460 470 480 490 500
HFRKTTDNPF KALGGNLVDM GRVKVIAGLL RKDDQEISST IRSIEQVFKL
510 520 530 540 550
VDQGEGFYQD GSYIDHTNVA YTGAYGNVLI DGLSQLLPVI QKTKNPIDKD
560 570 580 590 600
KMQTMYHWID KSFAPLLVNG ELMDMSRGRS ISRANSEGHV AAVEVLRGIH
610 620 630 640 650
RIADMSEGET KQCLQSLVKT IVQSDSYYDV FKNLKTYKDI SLMQSLLSDA
660 670 680 690 700
GVASVPRPSY LSAFNKMDKT AMYNAEKGFG FGLSLFSSRT LNYEHMNKEN
710 720 730 740 750
KRGWYTSDGM FYLYNGDLSH YSDGYWPTVN PYKMPGTTET DAKRADSDTG
760 770 780 790 800
KVLPSAFVGT SKLDDANATA TMDFTNWNQT LTAHKSWFML KDKIAFLGSN
810 820 830 840 850
IQNTSTDTAA TTIDQRKLES GNPYKVYVND KEASLTEQEK DYPETQSVFL
860 870 880 890 900
ESFDSKKNIG YFFFKKSSIS MSKALQKGAW KDINEGQSDK EVENEFLTIS
910 920 930 940 950
QAHKQNRDSY GYMLIPNVDR ATFNQMIKEL ESSLIENNET LQSVYDAKQG
960 970 980 990 1000
VWGIVKYDDS VSTISNQFQV LKRGVYTIRK EGDEYKIAYY NPETQESAPD
1010 1020 1030 1040 1050
QEVFKKLEQA AQPQVQNSKE KEKSEEEKNH SDQKNLPQTG EGQSILASLG
1060
FLLLGAFYLF RRGKNN
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. Curated
The sequence AAA53686.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081H → P(PubMed:8112843)Curated
Sequence conflicti115 – 1151L → V(PubMed:8112843)Curated
Sequence conflicti139 – 1391I → V in AAA53685. (PubMed:8112843)Curated
Sequence conflicti211 – 2111L → P in AAA53685. (PubMed:8112843)Curated
Sequence conflicti236 – 2361S → P in AAA53685. (PubMed:8112843)Curated
Sequence conflicti290 – 2901A → T in AAA53685. (PubMed:8112843)Curated
Sequence conflicti290 – 2901A → T in AAA53686. (PubMed:8112843)Curated
Sequence conflicti313 – 3131E → D in AAA53685. (PubMed:8112843)Curated
Sequence conflicti313 – 3131E → D in AAA53686. (PubMed:8112843)Curated
Sequence conflicti340 – 3401T → I in AAA53685. (PubMed:8112843)Curated
Sequence conflicti340 – 3401T → I in AAA53686. (PubMed:8112843)Curated
Sequence conflicti613 – 6131C → R in AAA53685. (PubMed:8112843)Curated
Sequence conflicti613 – 6131C → R in AAA53686. (PubMed:8112843)Curated
Sequence conflicti658 – 6581P → T in AAA53685. (PubMed:8112843)Curated
Sequence conflicti658 – 6581P → T in AAA53686. (PubMed:8112843)Curated
Sequence conflicti821 – 8211G → S in AAA53685. (PubMed:8112843)Curated
Sequence conflicti821 – 8211G → S in AAA53686. (PubMed:8112843)Curated
Sequence conflicti848 – 8481V → G in AAA53685. (PubMed:8112843)Curated
Sequence conflicti848 – 8481V → G in AAA53686. (PubMed:8112843)Curated
Sequence conflicti853 – 8531F → S in AAA53685. (PubMed:8112843)Curated
Sequence conflicti853 – 8531F → S in AAA53686. (PubMed:8112843)Curated
Sequence conflicti907 – 9071R → G in AAA53685. (PubMed:8112843)Curated
Sequence conflicti907 – 9071R → G in AAA53686. (PubMed:8112843)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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 [» ]
4D0Q X-ray 1.20 A 54-212 [» ]
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: November 26, 2014
This is version 125 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