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Main hemagglutinin component (HA 33 kDa subunit) (HA1)

 HA33_CLOBO              Reviewed;         286 AA.
P46084; Q9LBR3; Q9LBS9; Q9ZWV4;
01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 85.
RecName: Full=Main hemagglutinin component;
AltName: Full=HA 33 kDa subunit;
AltName: Full=HA1;
Name=HA-33; Synonyms=antP-33, ha1;
Clostridium botulinum.
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=1491;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=Type C / Stockholm;
PubMed=2205574;
Tsuzuki K., Kimura K., Fujii N., Yokosawa N., Indoh T., Murakami T.,
Oguma K.;
"Cloning and complete nucleotide sequence of the gene for the main
component of hemagglutinin produced by Clostridium botulinum type C.";
Infect. Immun. 58:3173-3177(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Type C / C-468;
PubMed=7570637; DOI=10.1016/0041-0101(94)00190-J;
Hauser D., Gibert M., Marvaud J.C., Eklund M.W., Popoff M.R.;
"Botulinal neurotoxin C1 complex genes, clostridial neurotoxin
homology and genetic transfer in Clostridium botulinum.";
Toxicon 33:515-526(1995).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Type D / D-1873;
PubMed=9802560; DOI=10.1111/j.1348-0421.1998.tb02330.x;
Nakajima H., Inoue K., Ikeda T., Fujinaga Y., Sunagawa H., Takeshi K.,
Ohyama T., Watanabe T., Inoue K., Oguma K.;
"Molecular composition of the 16S toxin produced by a Clostridium
botulinum type D strain, 1873.";
Microbiol. Immunol. 42:599-605(1998).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Type D / CB-16;
PubMed=8569530; DOI=10.1111/j.1348-0421.1995.tb02229.x;
Ohyama T., Watanabe T., Fujinaga Y., Inoue K., Sunagawa H., Fujii N.,
Oguma K.;
"Characterization of nontoxic-nonhemagglutinin component of the two
types of progenitor toxin (M and L) produced by Clostridium botulinum
type D CB-16.";
Microbiol. Immunol. 39:457-465(1995).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Type C / C-6814;
Sagane Y., Watanabe T., Kouguchi H., Yamamoto T., Kawabe T.,
Murakami F., Nakatsuka M., Ohyama T.;
"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.";
Submitted (JAN-2000) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=Type D / D-4947;
Sagane Y., Watanabe T., Kouguchi H., Yamamoto T., Takizawa J.,
Kawabe T., Murakami F., Muroga A., Nakatsuka M., Ohyama T.;
"Characterization of the progenitor toxin components produced by
Clostridium botulinum type D strain 4947.";
Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 269-286.
STRAIN=Type C / Stockholm;
PubMed=7802661; DOI=10.1006/bbrc.1994.2805;
Fujinaga Y., Inoue K., Shimazaki S., Tomochika K., Tsuzuki K.,
Fujii N., Watanabe T., Ohyama T., Takeshi K., Inoue K., Oguma K.;
"Molecular construction of Clostridium botulinum type C progenitor
toxin and its gene organization.";
Biochem. Biophys. Res. Commun. 205:1291-1298(1994).
[8]
ROLE IN TOXICITY.
STRAIN=Type C / Stockholm;
PubMed=9421908; DOI=10.1099/00221287-143-12-3841;
Fujinaga Y., Inoue K., Watanabe S., Yokota K., Hirai Y., Nagamachi E.,
Oguma K.;
"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.";
Microbiology 143:3841-3847(1997).
[9]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
STRAIN=Type C / Stockholm;
PubMed=14663070; DOI=10.1099/mic.0.26586-0;
Inoue K., Sobhany M., Transue T.R., Oguma K., Pedersen L.C.,
Negishi M.;
"Structural analysis by X-ray crystallography and calorimetry of a
haemagglutinin component (HA1) of the progenitor toxin from
Clostridium botulinum.";
Microbiology 149:3361-3370(2003).
-!- 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. {ECO:0000269|PubMed:9421908}.
-!- SUBUNIT: 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 CAUTION:
Sequence=BAA75077.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA75082.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X62389; CAA44261.1; -; Genomic_DNA.
EMBL; X53041; CAA37210.1; -; Genomic_DNA.
EMBL; X66433; CAA47058.1; -; Genomic_DNA.
EMBL; AB012112; BAA75082.1; ALT_INIT; Genomic_DNA.
EMBL; AB012111; BAA75077.1; ALT_INIT; Genomic_DNA.
EMBL; AB037166; BAA89711.1; -; Genomic_DNA.
EMBL; AB037920; BAA90659.1; -; Genomic_DNA.
EMBL; S74768; AAB32847.1; -; Genomic_DNA.
PDB; 1QXM; X-ray; 1.70 A; A/B=1-286.
PDB; 2E4M; X-ray; 1.85 A; A/B=1-286.
PDB; 3AH1; X-ray; 2.20 A; A/B=1-286.
PDB; 3AH2; X-ray; 1.70 A; A/B=1-286.
PDB; 3AH4; X-ray; 1.78 A; A/B=1-286.
PDB; 3AJ5; X-ray; 1.80 A; A/B=1-286.
PDB; 3AJ6; X-ray; 1.48 A; A/B=1-286.
PDBsum; 1QXM; -.
PDBsum; 2E4M; -.
PDBsum; 3AH1; -.
PDBsum; 3AH2; -.
PDBsum; 3AH4; -.
PDBsum; 3AJ5; -.
PDBsum; 3AJ6; -.
ProteinModelPortal; P46084; -.
SMR; P46084; -.
CAZy; CBM13; Carbohydrate-Binding Module Family 13.
EvolutionaryTrace; P46084; -.
GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
CDD; cd00161; RICIN; 2.
InterPro; IPR035992; Ricin_B-like_lectins.
InterPro; IPR000772; Ricin_B_lectin.
SMART; SM00458; RICIN; 2.
SUPFAM; SSF50370; SSF50370; 2.
PROSITE; PS50231; RICIN_B_LECTIN; 2.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Hemagglutinin; Lectin;
Repeat.
INIT_MET 1 1 Removed.
CHAIN 2 286 Main hemagglutinin component.
/FTId=PRO_0000083886.
DOMAIN 12 140 Ricin B-type lectin 1.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
DOMAIN 180 284 Ricin B-type lectin 2.
{ECO:0000255|PROSITE-ProRule:PRU00174}.
BINDING 28 28 Carbohydrate. {ECO:0000255}.
BINDING 45 45 Carbohydrate. {ECO:0000255}.
BINDING 256 256 Carbohydrate. {ECO:0000255}.
BINDING 271 271 Carbohydrate. {ECO:0000255}.
BINDING 278 278 Carbohydrate. {ECO:0000255}.
VARIANT 22 22 N -> S (in strain: Type C / C-6814).
VARIANT 39 44 NKLSGA -> SKNLGS (in strain: Type C / C-
6814).
VARIANT 60 60 K -> T (in strain: Type D / D-4947).
VARIANT 74 74 N -> D (in strain: Type C / C-6814 and
Type D / D-4947).
VARIANT 88 89 GD -> TN (in strain: Type C / C-6814 and
Type D / D-4947).
VARIANT 98 98 N -> D (in strain: Type C / C-6814 and
Type D / D-4947).
VARIANT 106 106 I -> L (in strain: Type C / C-6814 and
Type D / D-4947).
VARIANT 120 120 I -> T (in strain: Type C / C-6814 and
Type D / D-4947).
VARIANT 125 125 M -> I (in strain: Type C / C-6814 and
Type D / D-4947).
VARIANT 131 131 S -> N (in strain: Type D / D-4947).
VARIANT 133 133 S -> N (in strain: Type C / C-6814 and
Type D / D-4947).
VARIANT 187 187 I -> L (in strain: Type C / C-6814).
VARIANT 187 187 I -> T (in strain: Type D / D-4947).
VARIANT 262 262 I -> T (in strain: Type D / D-4947).
VARIANT 267 267 H -> N (in strain: Type C / C-6814).
STRAND 14 19 {ECO:0000244|PDB:3AJ6}.
STRAND 25 29 {ECO:0000244|PDB:3AJ6}.
STRAND 31 33 {ECO:0000244|PDB:3AJ6}.
STRAND 35 39 {ECO:0000244|PDB:3AJ6}.
HELIX 44 46 {ECO:0000244|PDB:3AJ6}.
STRAND 48 53 {ECO:0000244|PDB:3AJ6}.
TURN 54 57 {ECO:0000244|PDB:3AJ6}.
STRAND 58 67 {ECO:0000244|PDB:3AJ6}.
STRAND 70 73 {ECO:0000244|PDB:3AJ6}.
STRAND 80 83 {ECO:0000244|PDB:3AJ6}.
HELIX 89 91 {ECO:0000244|PDB:3AJ6}.
STRAND 93 97 {ECO:0000244|PDB:3AJ6}.
TURN 99 101 {ECO:0000244|PDB:3AJ6}.
STRAND 104 110 {ECO:0000244|PDB:3AJ6}.
STRAND 114 118 {ECO:0000244|PDB:3AJ6}.
STRAND 124 128 {ECO:0000244|PDB:3AJ6}.
HELIX 133 135 {ECO:0000244|PDB:3AJ6}.
STRAND 137 141 {ECO:0000244|PDB:3AJ6}.
HELIX 142 147 {ECO:0000244|PDB:3AJ6}.
STRAND 150 156 {ECO:0000244|PDB:3AJ6}.
STRAND 163 166 {ECO:0000244|PDB:3AJ6}.
STRAND 170 176 {ECO:0000244|PDB:3AJ6}.
HELIX 182 184 {ECO:0000244|PDB:3AJ6}.
STRAND 186 191 {ECO:0000244|PDB:3AJ6}.
TURN 192 195 {ECO:0000244|PDB:3AJ6}.
STRAND 196 201 {ECO:0000244|PDB:3AJ6}.
TURN 202 204 {ECO:0000244|PDB:3AJ6}.
STRAND 207 210 {ECO:0000244|PDB:3AJ6}.
STRAND 213 215 {ECO:0000244|PDB:3AH1}.
STRAND 217 221 {ECO:0000244|PDB:3AJ6}.
HELIX 227 229 {ECO:0000244|PDB:3AJ6}.
STRAND 231 236 {ECO:0000244|PDB:3AJ6}.
STRAND 239 247 {ECO:0000244|PDB:3AJ6}.
STRAND 250 257 {ECO:0000244|PDB:3AJ6}.
HELIX 258 260 {ECO:0000244|PDB:3AJ6}.
STRAND 267 272 {ECO:0000244|PDB:3AJ6}.
HELIX 277 279 {ECO:0000244|PDB:3AJ6}.
STRAND 281 285 {ECO:0000244|PDB:3AJ6}.
SEQUENCE 286 AA; 33753 MW; 221C2500C8B187EA CRC64;
MSQTNANDLR NNEVFFISPS NNTNKVLDKI SQSEVKLWNK LSGANQKWRL IYDTNKQAYK
IKVMDNTSLI LTWNAPLSSV SVKTDTNGDN QYWYLLQNYI SRNVIIRNYM NPNLVLQYNI
DDTLMVSTQT SSSNQFFKFS NCIYEALNNR NCKLQTQLNS DRFLSKNLNS QIIVLWQWFD
SSRQKWIIEY NETKSAYTLK CQENNRYLTW IQNSNNYVET YQSTDSLIQY WNINYLDNDA
SKYILYNLQD TNRVLDVYNS QIANGTHVIV DSYHGNTNQQ WIINLI


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