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Protein

Hyaluronate lyase

Gene

SP_0314

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

Functioni

Catalytic activityi

Cleaves hyaluronate chains at a beta-D-GlcNAc-(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)DescriptionActionsGraphical viewLength
Active sitei4661
Active sitei5161
Active sitei5251

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19222.
SPNE170187:GHGN-307-MONOMER.
BRENDAi4.2.2.1. 1960.
SABIO-RKQ54873.

Protein family/group databases

CAZyiCBM70. Carbohydrate-Binding Module Family 70.
PL8. 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
Proteomesi
  • UP000000585 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell wall, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi360R → V: Retains 67% of wild-type activity. 1 Publication1
Mutagenesisi466N → A: Almost complete loss of activity. 1 Publication1
Mutagenesisi516H → A: Almost complete loss of activity. 1 Publication1
Mutagenesisi525Y → F: Complete loss of activity. 1 Publication1
Mutagenesisi697N → G: Slightly increased activity. 1 Publication1

Chemistry databases

ChEMBLiCHEMBL1795158.
DrugBankiDB00126. Vitamin C.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 30Sequence analysisAdd BLAST30
ChainiPRO_000002493331 – 1039Hyaluronate lyaseAdd BLAST1009
PropeptideiPRO_00000249341040 – 1066Removed by sortaseSequence analysisAdd BLAST27

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1039Pentaglycyl murein peptidoglycan amidated threonineSequence analysis1

Keywords - PTMi

Peptidoglycan-anchor

Proteomic databases

PRIDEiQ54873.

Interactioni

Protein-protein interaction databases

STRINGi170187.SP_0314.

Chemistry databases

BindingDBiQ54873.

Structurei

Secondary structure

11066
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni57 – 60Combined sources4
Beta strandi63 – 65Combined sources3
Beta strandi80 – 83Combined sources4
Helixi85 – 87Combined sources3
Beta strandi95 – 99Combined sources5
Beta strandi102 – 120Combined sources19
Beta strandi127 – 150Combined sources24
Beta strandi153 – 158Combined sources6
Beta strandi162 – 175Combined sources14
Beta strandi182 – 206Combined sources25
Helixi290 – 302Combined sources13
Helixi305 – 307Combined sources3
Beta strandi310 – 312Combined sources3
Helixi313 – 332Combined sources20
Beta strandi336 – 338Combined sources3
Beta strandi340 – 342Combined sources3
Helixi344 – 346Combined sources3
Beta strandi349 – 351Combined sources3
Helixi353 – 369Combined sources17
Turni375 – 378Combined sources4
Helixi380 – 396Combined sources17
Beta strandi398 – 401Combined sources4
Helixi408 – 412Combined sources5
Helixi414 – 425Combined sources12
Helixi427 – 429Combined sources3
Helixi432 – 445Combined sources14
Beta strandi451 – 453Combined sources3
Beta strandi456 – 458Combined sources3
Helixi464 – 480Combined sources17
Helixi484 – 494Combined sources11
Helixi495 – 498Combined sources4
Beta strandi502 – 507Combined sources6
Beta strandi513 – 515Combined sources3
Turni516 – 518Combined sources3
Turni522 – 524Combined sources3
Helixi525 – 540Combined sources16
Beta strandi543 – 545Combined sources3
Helixi549 – 552Combined sources4
Helixi554 – 561Combined sources8
Helixi564 – 566Combined sources3
Helixi574 – 576Combined sources3
Helixi578 – 582Combined sources5
Helixi584 – 586Combined sources3
Helixi588 – 605Combined sources18
Helixi608 – 624Combined sources17
Beta strandi626 – 628Combined sources3
Helixi630 – 633Combined sources4
Helixi637 – 648Combined sources12
Beta strandi660 – 664Combined sources5
Helixi665 – 667Combined sources3
Beta strandi669 – 674Combined sources6
Turni675 – 678Combined sources4
Beta strandi679 – 684Combined sources6
Beta strandi690 – 692Combined sources3
Turni704 – 707Combined sources4
Beta strandi711 – 714Combined sources4
Turni718 – 721Combined sources4
Helixi725 – 728Combined sources4
Helixi731 – 733Combined sources3
Beta strandi738 – 740Combined sources3
Beta strandi758 – 760Combined sources3
Beta strandi767 – 775Combined sources9
Beta strandi779 – 789Combined sources11
Beta strandi794 – 803Combined sources10
Beta strandi805 – 807Combined sources3
Beta strandi809 – 817Combined sources9
Beta strandi820 – 822Combined sources3
Beta strandi825 – 828Combined sources4
Beta strandi831 – 833Combined sources3
Beta strandi840 – 851Combined sources12
Helixi855 – 857Combined sources3
Beta strandi859 – 878Combined sources20
Helixi880 – 882Combined sources3
Beta strandi892 – 902Combined sources11
Beta strandi908 – 917Combined sources10
Helixi920 – 929Combined sources10
Turni930 – 932Combined sources3
Beta strandi934 – 946Combined sources13
Turni947 – 950Combined sources4
Beta strandi951 – 958Combined sources8
Beta strandi962 – 964Combined sources3
Turni965 – 967Combined sources3
Beta strandi968 – 970Combined sources3
Beta strandi972 – 981Combined sources10
Beta strandi984 – 991Combined sources8
Turni992 – 995Combined sources4
Helixi1000 – 1003Combined sources4
Beta strandi1004 – 1006Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ54873.

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi1036 – 1040LPXTG sorting signalSequence analysis5

Sequence similaritiesi

Belongs to the polysaccharide lyase 8 family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiENOG4106AM8. Bacteria.
ENOG410XTFC. LUCA.
HOGENOMiHOG000008667.
KOiK01727.
OMAiRYYQDET.

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. GH-type_carb-bd.
IPR019948. Gram-positive_anchor.
IPR023295. Hyaluronate_lyase_beta_dom.
IPR014756. Ig_E-set.
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]
PfamiPF00746. Gram_pos_anchor. 1 hit.
PF02278. 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.

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 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAA53686 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti108H → P (PubMed:8112843).Curated1
Sequence conflicti115L → V (PubMed:8112843).Curated1
Sequence conflicti139I → V in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti211L → P in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti236S → P in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti290A → T in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti290A → T in AAA53686 (PubMed:8112843).Curated1
Sequence conflicti313E → D in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti313E → D in AAA53686 (PubMed:8112843).Curated1
Sequence conflicti340T → I in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti340T → I in AAA53686 (PubMed:8112843).Curated1
Sequence conflicti613C → R in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti613C → R in AAA53686 (PubMed:8112843).Curated1
Sequence conflicti658P → T in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti658P → T in AAA53686 (PubMed:8112843).Curated1
Sequence conflicti821G → S in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti821G → S in AAA53686 (PubMed:8112843).Curated1
Sequence conflicti848V → G in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti848V → G in AAA53686 (PubMed:8112843).Curated1
Sequence conflicti853F → S in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti853F → S in AAA53686 (PubMed:8112843).Curated1
Sequence conflicti907R → G in AAA53685 (PubMed:8112843).Curated1
Sequence conflicti907R → G in AAA53686 (PubMed:8112843).Curated1

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.
RefSeqiWP_001193686.1. NZ_AKVY01000001.1.

Genome annotation databases

EnsemblBacteriaiAAK74491; AAK74491; SP_0314.
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.
PIRiB95037.
RefSeqiWP_001193686.1. NZ_AKVY01000001.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi170187.SP_0314.

Chemistry databases

BindingDBiQ54873.
ChEMBLiCHEMBL1795158.
DrugBankiDB00126. Vitamin C.

Protein family/group databases

CAZyiCBM70. Carbohydrate-Binding Module Family 70.
PL8. Polysaccharide Lyase Family 8.

Proteomic databases

PRIDEiQ54873.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiENOG4106AM8. Bacteria.
ENOG410XTFC. LUCA.
HOGENOMiHOG000008667.
KOiK01727.
OMAiRYYQDET.

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-19222.
SPNE170187:GHGN-307-MONOMER.
BRENDAi4.2.2.1. 1960.
SABIO-RKQ54873.

Miscellaneous databases

EvolutionaryTraceiQ54873.
PROiQ54873.

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. GH-type_carb-bd.
IPR019948. Gram-positive_anchor.
IPR023295. Hyaluronate_lyase_beta_dom.
IPR014756. Ig_E-set.
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]
PfamiPF00746. Gram_pos_anchor. 1 hit.
PF02278. 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.
ProtoNetiSearch...

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 2, 2016
This is version 140 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.