HA33D_CBDP
ID HA33D_CBDP Reviewed; 286 AA.
AC P0DPR1; P46084; Q9LBR3; Q9LBS9; Q9ZWV4;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 25-MAY-2022, entry version 14.
DE RecName: Full=Main hemagglutinin component type D;
DE AltName: Full=HA 33 kDa subunit {ECO:0000303|PubMed:8569530};
DE AltName: Full=HA1 {ECO:0000303|PubMed:8569530};
GN Name=ha-33 {ECO:0000303|PubMed:8569530}; Synonyms=antP-33, ha1;
OS Clostridium botulinum D phage (Clostridium botulinum D bacteriophage).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Siphoviridae.
OX NCBI_TaxID=29342;
OH NCBI_TaxID=1491; Clostridium botulinum.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-16, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=CB-16 / Type D / phage d-16 phi;
RX PubMed=8569530; DOI=10.1111/j.1348-0421.1995.tb02229.x;
RA Ohyama T., Watanabe T., Fujinaga Y., Inoue K., Sunagawa H., Fujii N.,
RA Oguma K.;
RT "Characterization of nontoxic-nonhemagglutinin component of the two types
RT of progenitor toxin (M and L) produced by Clostridium botulinum type D CB-
RT 16.";
RL Microbiol. Immunol. 39:457-465(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=D-4947 / Type D;
RX PubMed=11713244; DOI=10.1074/jbc.m106762200;
RA Kouguchi H., Watanabe T., Sagane Y., Sunagawa H., Ohyama T.;
RT "In vitro reconstitution of the Clostridium botulinum type D progenitor
RT toxin.";
RL J. Biol. Chem. 277:2650-2656(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11, SUBUNIT, AND
RP SUBCELLULAR LOCATION.
RC STRAIN=CB-16 / Type D, and D-1873 / Type D;
RX PubMed=9802560; DOI=10.1111/j.1348-0421.1998.tb02330.x;
RA Nakajima H., Inoue K., Ikeda T., Fujinaga Y., Sunagawa H., Takeshi K.,
RA Ohyama T., Watanabe T., Inoue K., Oguma K.;
RT "Molecular composition of the 16S toxin produced by a Clostridium botulinum
RT type D strain, 1873.";
RL Microbiol. Immunol. 42:599-605(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=D-4947 / Type D;
RA Sagane Y., Watanabe T., Kouguchi H., Yamamoto T., Takizawa J., Kawabe T.,
RA Murakami F., Muroga A., Nakatsuka M., Ohyama T.;
RT "Characterization of the progenitor toxin components produced by
RT Clostridium botulinum type D strain 4947.";
RL Submitted (FEB-2000) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0007744|PDB:2E4M}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH HA-17, PROTEIN
RP SEQUENCE OF 2-6, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=D-4947 / Type D;
RX PubMed=17581814; DOI=10.1074/jbc.m703446200;
RA Hasegawa K., Watanabe T., Suzuki T., Yamano A., Oikawa T., Sato Y.,
RA Kouguchi H., Yoneyama T., Niwa K., Ikeda T., Ohyama T.;
RT "A novel subunit structure of Clostridium botulinum serotype D toxin
RT complex with three extended arms.";
RL J. Biol. Chem. 282:24777-24783(2007).
CC -!- FUNCTION: The hemagglutinin (HA) component of the progenitor toxin
CC protects the structural integrity of the neurotoxin; may increase
CC internalization of the neurotoxin into the bloodstream of the host.
CC Involved in binding to the small intestine through interactions with
CC glycolipids and glycoproteins containing sialic acid moieties (By
CC similarity). Erythrocyte agglutination only occurs when the entire
CC complex is assembled (PubMed:17581814). Binds eukaryotic host mucins as
CC well as N-acetyl-beta-neuraminic acid, N-acetyl-D-galactosamine and
CC galactose (but not glucose) via 2 sites (By similarity).
CC {ECO:0000250|UniProtKB:P0DPR0, ECO:0000269|PubMed:17581814}.
CC -!- SUBUNIT: Botulinum toxins are produced as large progenitor toxins of
CC 12S (M toxin, about 280 kDa) and 16S (L toxin, about 650 kDa). M toxin
CC consists of a non-toxic, non-hemagglutinin component (NTNHA) and the
CC neurotoxin (PubMed:8569530, PubMed:11713244, PubMed:17581814). L toxin
CC consists of the M toxin and the 3 subcomponents of hemagglutinin (HA)
CC (PubMed:8569530, PubMed:11713244, PubMed:9802560, PubMed:17581814). HA
CC is composed of subcomponents of 70, 33, and 17 kDa (PubMed:17581814).
CC The stoichiometry of the whole complex has been modeled as one BoNT/D,
CC one NTNHA, three HA-70, six HA-33 and three HA-17 (PubMed:17581814).
CC HA-33 and HA-17 crystallize as a heterotrimer with two HA-33 and one
CC HA-17 (PubMed:17581814). {ECO:0000269|PubMed:11713244,
CC ECO:0000269|PubMed:17581814, ECO:0000269|PubMed:8569530,
CC ECO:0000269|PubMed:9802560}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11713244,
CC ECO:0000269|PubMed:17581814, ECO:0000269|PubMed:8569530,
CC ECO:0000269|PubMed:9802560}.
CC -!- DOMAIN: Arranged in 2 beta-trefoil domains (called 1 and 2) each with
CC three tandemly repeated subdomains (called alpha, beta and gamma)
CC joined by a short alpha-helix (By similarity). Only subdomains 2-alpha
CC and 2-gamma, in the C-terminal beta-trefoil domain, possess a
CC functional carbohydrate-binding site (By similarity).
CC {ECO:0000250|UniProtKB:P0DPR0}.
CC -!- MISCELLANEOUS: This protein can also be encoded on a prophage.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA75077.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAA75082.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB012112; BAA75082.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB012111; BAA75077.1; ALT_INIT; Genomic_DNA.
DR EMBL; AB037920; BAA90659.1; -; Genomic_DNA.
DR PDB; 2E4M; X-ray; 1.85 A; A/B=1-286.
DR PDBsum; 2E4M; -.
DR SMR; P0DPR1; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR CDD; cd00161; RICIN; 2.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR InterPro; IPR000772; Ricin_B_lectin.
DR SMART; SM00458; RICIN; 2.
DR SUPFAM; SSF50370; SSF50370; 2.
DR PROSITE; PS50231; RICIN_B_LECTIN; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hemagglutinin; Lectin; Repeat;
KW Secreted; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11713244,
FT ECO:0000269|PubMed:8569530, ECO:0000269|PubMed:9802560"
FT CHAIN 2..286
FT /note="Main hemagglutinin component type D"
FT /id="PRO_0000445709"
FT REPEAT 2..55
FT /note="1-alpha"
FT /evidence="ECO:0000250|UniProtKB:P0DPR0"
FT DOMAIN 12..140
FT /note="Ricin B-type lectin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 56..100
FT /note="1-beta"
FT /evidence="ECO:0000250|UniProtKB:P0DPR0"
FT REPEAT 101..148
FT /note="1-gamma"
FT /evidence="ECO:0000250|UniProtKB:P0DPR0"
FT REPEAT 149..193
FT /note="2-alpha"
FT /evidence="ECO:0000250|UniProtKB:P0DPR0"
FT DOMAIN 180..284
FT /note="Ricin B-type lectin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00174"
FT REPEAT 194..239
FT /note="2-beta"
FT /evidence="ECO:0000250|UniProtKB:P0DPR0"
FT REPEAT 240..286
FT /note="2-gamma"
FT /evidence="ECO:0000250|UniProtKB:P0DPR0"
FT REGION 167..183
FT /note="Sugar-binding site 1"
FT /evidence="ECO:0000250|UniProtKB:P0DPR0"
FT REGION 256..279
FT /note="Sugar-binding site 2"
FT /evidence="ECO:0000250|UniProtKB:P0DPR0"
FT VARIANT 60
FT /note="K -> T (in strain: Type D / D-4947)"
FT VARIANT 74
FT /note="N -> D (in strain: Type D / D-4947)"
FT VARIANT 88..89
FT /note="GD -> TN (in strain: Type D / D-4947)"
FT VARIANT 98
FT /note="N -> D (in strain: Type D / D-4947)"
FT VARIANT 106
FT /note="I -> L (in strain: Type D / D-4947)"
FT VARIANT 120
FT /note="I -> T (in strain: Type D / D-4947)"
FT VARIANT 125
FT /note="M -> I (in strain: Type D / D-4947)"
FT VARIANT 131
FT /note="S -> N (in strain: Type D / D-4947)"
FT VARIANT 133
FT /note="S -> N (in strain: Type D / D-4947)"
FT VARIANT 187
FT /note="I -> T (in strain: Type D / D-4947)"
FT VARIANT 262
FT /note="I -> T (in strain: Type D / D-4947)"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 35..39
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:2E4M"
FT TURN 54..57
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 58..63
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 70..73
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 77..83
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 93..98
FT /evidence="ECO:0007829|PDB:2E4M"
FT TURN 99..101
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 104..110
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 115..118
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 124..127
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 142..147
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 150..156
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 163..166
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 170..176
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 186..191
FT /evidence="ECO:0007829|PDB:2E4M"
FT TURN 192..195
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 196..201
FT /evidence="ECO:0007829|PDB:2E4M"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 207..210
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 217..221
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 227..229
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 231..236
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 239..247
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 253..257
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 281..285
FT /evidence="ECO:0007829|PDB:2E4M"
SQ 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
