Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei28 – 281CarbohydrateSequence analysis
Binding sitei45 – 451CarbohydrateSequence analysis
Binding sitei256 – 2561CarbohydrateSequence analysis
Binding sitei271 – 2711CarbohydrateSequence analysis
Binding sitei278 – 2781CarbohydrateSequence analysis

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)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved
Chaini2 – 286285Main hemagglutinin componentPRO_0000083886Add
BLAST

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

1
286
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi14 – 196Combined sources
Beta strandi25 – 295Combined sources
Beta strandi31 – 333Combined sources
Beta strandi35 – 395Combined sources
Helixi44 – 463Combined sources
Beta strandi48 – 536Combined sources
Turni54 – 574Combined sources
Beta strandi58 – 6710Combined sources
Beta strandi70 – 734Combined sources
Beta strandi80 – 834Combined sources
Helixi89 – 913Combined sources
Beta strandi93 – 975Combined sources
Turni99 – 1013Combined sources
Beta strandi104 – 1107Combined sources
Beta strandi114 – 1185Combined sources
Beta strandi124 – 1285Combined sources
Helixi133 – 1353Combined sources
Beta strandi137 – 1415Combined sources
Helixi142 – 1476Combined sources
Beta strandi150 – 1567Combined sources
Beta strandi163 – 1664Combined sources
Beta strandi170 – 1767Combined sources
Helixi182 – 1843Combined sources
Beta strandi186 – 1916Combined sources
Turni192 – 1954Combined sources
Beta strandi196 – 2016Combined sources
Turni202 – 2043Combined sources
Beta strandi207 – 2104Combined sources
Beta strandi213 – 2153Combined sources
Beta strandi217 – 2215Combined sources
Helixi227 – 2293Combined sources
Beta strandi231 – 2366Combined sources
Beta strandi239 – 2479Combined sources
Beta strandi250 – 2578Combined sources
Helixi258 – 2603Combined sources
Beta strandi267 – 2726Combined sources
Helixi277 – 2793Combined sources
Beta strandi281 – 2855Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-286.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP46084.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini12 – 140129Ricin B-type lectin 1PROSITE-ProRule annotationAdd
BLAST
Domaini180 – 284105Ricin B-type lectin 2PROSITE-ProRule annotationAdd
BLAST

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)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti22 – 221N → S in strain: Type C / C-6814.
Natural varianti39 – 446NKLSGA → SKNLGS in strain: Type C / C-6814.
Natural varianti60 – 601K → T in strain: Type D / D-4947.
Natural varianti74 – 741N → D in strain: Type C / C-6814 and Type D / D-4947.
Natural varianti88 – 892GD → TN in strain: Type C / C-6814 and Type D / D-4947.
Natural varianti98 – 981N → D in strain: Type C / C-6814 and Type D / D-4947.
Natural varianti106 – 1061I → L in strain: Type C / C-6814 and Type D / D-4947.
Natural varianti120 – 1201I → T in strain: Type C / C-6814 and Type D / D-4947.
Natural varianti125 – 1251M → I in strain: Type C / C-6814 and Type D / D-4947.
Natural varianti131 – 1311S → N in strain: Type D / D-4947.
Natural varianti133 – 1331S → N in strain: Type C / C-6814 and Type D / D-4947.
Natural varianti187 – 1871I → L in strain: Type C / C-6814.
Natural varianti187 – 1871I → T in strain: Type D / D-4947.
Natural varianti262 – 2621I → T in strain: Type D / D-4947.
Natural varianti267 – 2671H → N in strain: Type C / C-6814.

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
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. Positions 1-286.
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: September 7, 2016
This is version 81 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.