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Protein

Main hemagglutinin component

Gene

HA-33

Organism
Clostridium botulinum
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Protects the structural integrity of the neurotoxin; may increase internalization of the neurotoxin into the bloodstream of the host. Involved in binding to the small intestine through interactions with glycolipids and glycoproteins containing sialic acid moieties.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei28CarbohydrateSequence analysis1
Binding sitei45CarbohydrateSequence analysis1
Binding sitei256CarbohydrateSequence analysis1
Binding sitei271CarbohydrateSequence analysis1
Binding sitei278CarbohydrateSequence analysis1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hemagglutinin

Keywords - Ligandi

Lectin

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Names & Taxonomyi

Protein namesi
Recommended name:
Main hemagglutinin component
Alternative name(s):
HA 33 kDa subunit
HA1
Gene namesi
Name:HA-33
Synonyms:antP-33, ha1
OrganismiClostridium botulinum
Taxonomic identifieri1491 [NCBI]
Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesClostridiaceaeClostridium

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved
ChainiPRO_00000838862 – 286Main hemagglutinin componentAdd BLAST285

Interactioni

Subunit structurei

Botulinum toxins are produced as progenitor toxins of large molecular sizes of 12S (M toxin), 16S (L toxin) and 19S (LL toxin). M toxin consists of a nontoxic, non-hemagglutinin component (NTNHA) and the neurotoxin. L toxin consists of the M toxin and the 3 subcomponents of hemagglutinin (HA). HA is composed of subcomponents having 70, 33, and 17 kDa. The 70 kDa subcomponent undergoes proteolytic processing and is split into HA-55 and HA-22-23.

Structurei

Secondary structure

1286
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi14 – 19Combined sources6
Beta strandi25 – 29Combined sources5
Beta strandi31 – 33Combined sources3
Beta strandi35 – 39Combined sources5
Helixi44 – 46Combined sources3
Beta strandi48 – 53Combined sources6
Turni54 – 57Combined sources4
Beta strandi58 – 67Combined sources10
Beta strandi70 – 73Combined sources4
Beta strandi80 – 83Combined sources4
Helixi89 – 91Combined sources3
Beta strandi93 – 97Combined sources5
Turni99 – 101Combined sources3
Beta strandi104 – 110Combined sources7
Beta strandi114 – 118Combined sources5
Beta strandi124 – 128Combined sources5
Helixi133 – 135Combined sources3
Beta strandi137 – 141Combined sources5
Helixi142 – 147Combined sources6
Beta strandi150 – 156Combined sources7
Beta strandi163 – 166Combined sources4
Beta strandi170 – 176Combined sources7
Helixi182 – 184Combined sources3
Beta strandi186 – 191Combined sources6
Turni192 – 195Combined sources4
Beta strandi196 – 201Combined sources6
Turni202 – 204Combined sources3
Beta strandi207 – 210Combined sources4
Beta strandi213 – 215Combined sources3
Beta strandi217 – 221Combined sources5
Helixi227 – 229Combined sources3
Beta strandi231 – 236Combined sources6
Beta strandi239 – 247Combined sources9
Beta strandi250 – 257Combined sources8
Helixi258 – 260Combined sources3
Beta strandi267 – 272Combined sources6
Helixi277 – 279Combined sources3
Beta strandi281 – 285Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QXMX-ray1.70A/B1-286[»]
2E4MX-ray1.85A/B1-286[»]
3AH1X-ray2.20A/B1-286[»]
3AH2X-ray1.70A/B1-286[»]
3AH4X-ray1.78A/B1-286[»]
3AJ5X-ray1.80A/B1-286[»]
3AJ6X-ray1.48A/B1-286[»]
ProteinModelPortaliP46084.
SMRiP46084.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46084.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini12 – 140Ricin B-type lectin 1PROSITE-ProRule annotationAdd BLAST129
Domaini180 – 284Ricin B-type lectin 2PROSITE-ProRule annotationAdd BLAST105

Sequence similaritiesi

Contains 2 ricin B-type lectin domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Family and domain databases

InterProiIPR000772. Ricin_B_lectin.
[Graphical view]
SMARTiSM00458. RICIN. 2 hits.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 2 hits.
PROSITEiPS50231. RICIN_B_LECTIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P46084-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQTNANDLR NNEVFFISPS NNTNKVLDKI SQSEVKLWNK LSGANQKWRL
60 70 80 90 100
IYDTNKQAYK IKVMDNTSLI LTWNAPLSSV SVKTDTNGDN QYWYLLQNYI
110 120 130 140 150
SRNVIIRNYM NPNLVLQYNI DDTLMVSTQT SSSNQFFKFS NCIYEALNNR
160 170 180 190 200
NCKLQTQLNS DRFLSKNLNS QIIVLWQWFD SSRQKWIIEY NETKSAYTLK
210 220 230 240 250
CQENNRYLTW IQNSNNYVET YQSTDSLIQY WNINYLDNDA SKYILYNLQD
260 270 280
TNRVLDVYNS QIANGTHVIV DSYHGNTNQQ WIINLI
Length:286
Mass (Da):33,753
Last modified:January 23, 2007 - v3
Checksum:i221C2500C8B187EA
GO

Sequence cautioni

The sequence BAA75077 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA75082 differs from that shown. Reason: Erroneous initiation.Curated

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti22N → S in strain: Type C / C-6814. 1
Natural varianti39 – 44NKLSGA → SKNLGS in strain: Type C / C-6814. 6
Natural varianti60K → T in strain: Type D / D-4947. 1
Natural varianti74N → D in strain: Type C / C-6814 and Type D / D-4947. 1
Natural varianti88 – 89GD → TN in strain: Type C / C-6814 and Type D / D-4947. 2
Natural varianti98N → D in strain: Type C / C-6814 and Type D / D-4947. 1
Natural varianti106I → L in strain: Type C / C-6814 and Type D / D-4947. 1
Natural varianti120I → T in strain: Type C / C-6814 and Type D / D-4947. 1
Natural varianti125M → I in strain: Type C / C-6814 and Type D / D-4947. 1
Natural varianti131S → N in strain: Type D / D-4947. 1
Natural varianti133S → N in strain: Type C / C-6814 and Type D / D-4947. 1
Natural varianti187I → L in strain: Type C / C-6814. 1
Natural varianti187I → T in strain: Type D / D-4947. 1
Natural varianti262I → T in strain: Type D / D-4947. 1
Natural varianti267H → N in strain: Type C / C-6814. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62389 Genomic DNA. Translation: CAA44261.1.
X53041 Genomic DNA. Translation: CAA37210.1.
X66433 Genomic DNA. Translation: CAA47058.1.
AB012112 Genomic DNA. Translation: BAA75082.1. Different initiation.
AB012111 Genomic DNA. Translation: BAA75077.1. Different initiation.
AB037166 Genomic DNA. Translation: BAA89711.1.
AB037920 Genomic DNA. Translation: BAA90659.1.
S74768 Genomic DNA. Translation: AAB32847.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X62389 Genomic DNA. Translation: CAA44261.1.
X53041 Genomic DNA. Translation: CAA37210.1.
X66433 Genomic DNA. Translation: CAA47058.1.
AB012112 Genomic DNA. Translation: BAA75082.1. Different initiation.
AB012111 Genomic DNA. Translation: BAA75077.1. Different initiation.
AB037166 Genomic DNA. Translation: BAA89711.1.
AB037920 Genomic DNA. Translation: BAA90659.1.
S74768 Genomic DNA. Translation: AAB32847.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1QXMX-ray1.70A/B1-286[»]
2E4MX-ray1.85A/B1-286[»]
3AH1X-ray2.20A/B1-286[»]
3AH2X-ray1.70A/B1-286[»]
3AH4X-ray1.78A/B1-286[»]
3AJ5X-ray1.80A/B1-286[»]
3AJ6X-ray1.48A/B1-286[»]
ProteinModelPortaliP46084.
SMRiP46084.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiCBM13. Carbohydrate-Binding Module Family 13.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP46084.

Family and domain databases

InterProiIPR000772. Ricin_B_lectin.
[Graphical view]
SMARTiSM00458. RICIN. 2 hits.
[Graphical view]
SUPFAMiSSF50370. SSF50370. 2 hits.
PROSITEiPS50231. RICIN_B_LECTIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiHA33_CLOBO
AccessioniPrimary (citable) accession number: P46084
Secondary accession number(s): Q9LBR3, Q9LBS9, Q9ZWV4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 83 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

This protein is encoded on a prophage.

Keywords - Technical termi

3D-structure, Direct protein sequencing

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.