P46084 (HA33_CLOBO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Main hemagglutinin component

Alternative name(s):
HA 33 kDa subunit
HA1

Gene names

Name:	HA-33
Synonyms:	antP-33, ha1

Organism

Clostridium botulinum

Taxonomic identifier

1491 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	286 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.8
Subunit structure	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.
Miscellaneous	This protein is encoded on a prophage.
Sequence similarities	Contains 2 ricin B-type lectin domains.
Sequence caution	The sequence BAA75077.1 differs from that shown. Reason: Erroneous initiation. The sequence BAA75082.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Domain	Repeat
Ligand	Lectin
Molecular function	Hemagglutinin
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Molecular function	sugar binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed

Chain

2 – 286

285

Main hemagglutinin component

PRO_0000083886

Regions

Domain

12 – 140

129

Ricin B-type lectin 1

Domain

180 – 284

105

Ricin B-type lectin 2

Sites

Binding site

28

1

Carbohydrate Potential

Binding site

45

1

Carbohydrate Potential

Binding site

256

1

Carbohydrate Potential

Binding site

271

1

Carbohydrate Potential

Binding site

278

1

Carbohydrate Potential

Natural variations

Natural variant

22

1

N → S in strain: Type C / C-6814.

Natural variant

39 – 44

6

NKLSGA → SKNLGS in strain: Type C / C-6814.

Natural variant

60

1

K → T in strain: Type D / D-4947.

Natural variant

74

1

N → D in strain: Type C / C-6814 and Type D / D-4947.

Natural variant

88 – 89

2

GD → TN in strain: Type C / C-6814 and Type D / D-4947.

Natural variant

98

1

N → D in strain: Type C / C-6814 and Type D / D-4947.

Natural variant

106

1

I → L in strain: Type C / C-6814 and Type D / D-4947.

Natural variant

120

1

I → T in strain: Type C / C-6814 and Type D / D-4947.

Natural variant

125

1

M → I in strain: Type C / C-6814 and Type D / D-4947.

Natural variant

131

1

S → N in strain: Type D / D-4947.

Natural variant

133

1

S → N in strain: Type C / C-6814 and Type D / D-4947.

Natural variant

187

1

I → L in strain: Type C / C-6814.

Natural variant

187

1

I → T in strain: Type D / D-4947.

Natural variant

262

1

I → T in strain: Type D / D-4947.

Natural variant

267

1

H → N in strain: Type C / C-6814.

Secondary structure

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286

Helix Strand Turn

Details...

Beta strand

14 – 19

6

Beta strand

25 – 29

5

Beta strand

31 – 33

3

Beta strand

35 – 39

5

Helix

44 – 46

3

Beta strand

48 – 53

6

Turn

54 – 57

4

Beta strand

58 – 63

6

Beta strand

65 – 67

3

Beta strand

70 – 73

4

Beta strand

77 – 83

7

Helix

89 – 91

3

Beta strand

93 – 98

6

Turn

99 – 101

3

Beta strand

104 – 110

7

Beta strand

115 – 118

4

Beta strand

124 – 127

4

Helix

133 – 135

3

Beta strand

137 – 141

5

Helix

142 – 147

6

Beta strand

150 – 156

7

Beta strand

163 – 166

4

Beta strand

170 – 176

7

Helix

182 – 184

3

Beta strand

186 – 191

6

Turn

192 – 195

4

Beta strand

196 – 201

6

Turn

202 – 204

3

Beta strand

207 – 210

4

Beta strand

217 – 221

5

Helix

227 – 229

3

Beta strand

231 – 236

6

Beta strand

239 – 247

9

Beta strand

253 – 257

5

Helix

258 – 260

3

Beta strand

267 – 272

6

Helix

277 – 279

3

Beta strand

281 – 285

5

Sequences

	Sequence		Length	Mass (Da)
	P46084 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 221C2500C8B187EA	FASTA	286	33,753
	10 20 30 40 50 60 MSQTNANDLR NNEVFFISPS NNTNKVLDKI SQSEVKLWNK LSGANQKWRL IYDTNKQAYK 70 80 90 100 110 120 IKVMDNTSLI LTWNAPLSSV SVKTDTNGDN QYWYLLQNYI SRNVIIRNYM NPNLVLQYNI 130 140 150 160 170 180 DDTLMVSTQT SSSNQFFKFS NCIYEALNNR NCKLQTQLNS DRFLSKNLNS QIIVLWQWFD 190 200 210 220 230 240 SSRQKWIIEY NETKSAYTLK CQENNRYLTW IQNSNNYVET YQSTDSLIQY WNINYLDNDA 250 260 270 280 SKYILYNLQD TNRVLDVYNS QIANGTHVIV DSYHGNTNQQ WIINLI

References

[1]	"Cloning and complete nucleotide sequence of the gene for the main component of hemagglutinin produced by Clostridium botulinum type C." Tsuzuki K., Kimura K., Fujii N., Yokosawa N., Indoh T., Murakami T., Oguma K. Infect. Immun. 58:3173-3177(1990) [PubMed: 2205574] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: Type C / Stockholm.
[2]	"Botulinal neurotoxin C1 complex genes, clostridial neurotoxin homology and genetic transfer in Clostridium botulinum." Hauser D., Gibert M., Marvaud J.C., Eklund M.W., Popoff M.R. Toxicon 33:515-526(1995) [PubMed: 7570637] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Type C / C-468.
[3]	"Molecular composition of the 16S toxin produced by a Clostridium botulinum type D strain, 1873." Nakajima H., Inoue K., Ikeda T., Fujinaga Y., Sunagawa H., Takeshi K., Ohyama T., Watanabe T., Inoue K., Oguma K. Microbiol. Immunol. 42:599-605(1998) [PubMed: 9802560] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Type D / D-1873.
[4]	"Characterization of nontoxic-nonhemagglutinin component of the two types of progenitor toxin (M and L) produced by Clostridium botulinum type D CB-16." Ohyama T., Watanabe T., Fujinaga Y., Inoue K., Sunagawa H., Fujii N., Oguma K. Microbiol. Immunol. 39:457-465(1995) [PubMed: 8569530] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Type D / CB-16.
[5]	"Organization of gene encoding components of the botulinum progenitor toxin in Clostridium botulinum type C strain 6814: evidence of chimeric sequence in the gene encoding each component." Sagane Y., Watanabe T., Kouguchi H., Yamamoto T., Kawabe T., Murakami F., Nakatsuka M., Ohyama T. Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Type C / C-6814.
[6]	"Characterization of the progenitor toxin components produced by Clostridium botulinum type D strain 4947." Sagane Y., Watanabe T., Kouguchi H., Yamamoto T., Takizawa J., Kawabe T., Murakami F., Muroga A., Nakatsuka M., Ohyama T. Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: Type D / D-4947.
[7]	"Molecular construction of Clostridium botulinum type C progenitor toxin and its gene organization." Fujinaga Y., Inoue K., Shimazaki S., Tomochika K., Tsuzuki K., Fujii N., Watanabe T., Ohyama T., Takeshi K., Inoue K., Oguma K. Biochem. Biophys. Res. Commun. 205:1291-1298(1994) [PubMed: 7802661] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 269-286. Strain: Type C / Stockholm.
[8]	"The haemagglutinin of Clostridium botulinum type C progenitor toxin plays an essential role in binding of toxin to the epithelial cells of guinea pig small intestine, leading to the efficient absorption of the toxin." Fujinaga Y., Inoue K., Watanabe S., Yokota K., Hirai Y., Nagamachi E., Oguma K. Microbiology 143:3841-3847(1997) [PubMed: 9421908] [Abstract] Cited for: ROLE IN TOXICITY. Strain: Type C / Stockholm.
[9]	"Structural analysis by X-ray crystallography and calorimetry of a haemagglutinin component (HA1) of the progenitor toxin from Clostridium botulinum." Inoue K., Sobhany M., Transue T.R., Oguma K., Pedersen L.C., Negishi M. Microbiology 149:3361-3370(2003) [PubMed: 14663070] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). Strain: Type C / Stockholm.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1QXM	X-ray	1.70	A/B	1-286	[»]
2E4M	X-ray	1.85	A/B	2-285	[»]
3AH1	X-ray	2.20	A/B	1-286	[»]
3AH2	X-ray	1.70	A/B	1-286	[»]
3AH4	X-ray	1.78	A/B	1-286	[»]
3AJ5	X-ray	1.80	A/B	1-286	[»]
3AJ6	X-ray	1.48	A/B	1-286	[»]

ProteinModelPortal

P46084.

SMR

P46084. Positions 1-286.

ModBase

Search...

Protein family/group databases

CAZy

CBM13. Carbohydrate-Binding Module Family 13.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR008997. Ricin_B-rel_lectin.
IPR000772. Ricin_B_lectin.
[Graphical view]

Pfam

PF00652. Ricin_B_lectin. 1 hit.
[Graphical view]

SMART

SM00458. RICIN. 2 hits.
[Graphical view]

SUPFAM

SSF50370. RicinB_like. 2 hits.

PROSITE

PS50231. RICIN_B_LECTIN. 2 hits.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

HA33_CLOBO

Accession

Primary (citable) accession number: P46084
Secondary accession number(s): Q9LBR3, Q9LBS9, Q9ZWV4

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1995
Last sequence update:	January 23, 2007
Last modified:	July 27, 2011
This is version 64 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program