HA17D_CBDP
ID HA17D_CBDP Reviewed; 146 AA.
AC Q9LBR4;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 29-SEP-2021, entry version 65.
DE RecName: Full=Hemagglutinin component HA-17 type D;
DE AltName: Full=ANTP17;
DE AltName: Full=HA 17 kDa subunit;
DE AltName: Full=HA2 {ECO:0000303|PubMed:8569530};
GN Name=ha-17 {ECO:0000303|PubMed:11713244};
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 2-11, FUNCTION,
RP SUBUNIT, AND 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 [2]
RP PROTEIN SEQUENCE OF 2-16, SUBUNIT, AND 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 [3] {ECO:0007744|PDB:2E4M}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH HA-33, PROTEIN
RP SEQUENCE OF 2-6, FUNCTION, 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 (By
CC similarity). Involved in binding to the small intestine through
CC interactions with glycolipids and glycoproteins containing sialic acid
CC moieties (Probable). The hemagglutinin complex composed of HA-70, HA-33
CC and HA-17 agglutinates erythrocytes, whereas the individual compenents
CC do not (PubMed:11713244). Erythrocyte agglutination also occurs with
CC the entire toxin complex (PubMed:11713244, PubMed:17581814).
CC {ECO:0000250|UniProtKB:P46083, ECO:0000269|PubMed:11713244,
CC ECO:0000269|PubMed:17581814, ECO:0000305}.
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)
CC (PubMed:11713244, PubMed:17581814). M toxin consists of a non-toxic,
CC non-hemagglutinin component (NTNHA) and the neurotoxin (BoNT/D)
CC (PubMed:8569530, PubMed:11713244, PubMed:17581814). L toxin consists of
CC the M toxin and the 3 hemagglutinin (HA) subcomponents of 70, 33, and
CC 17 kDa (PubMed:8569530, PubMed:17581814, PubMed:11713244). The
CC stoichiometry of the whole complex has been modeled as one BoNT/D, one
CC NTNHA, three HA-70, six HA-33 and three HA-17 (PubMed:17581814). HA-33
CC and HA-17 crystallize as a heterotrimer with two HA-33 and one HA-17
CC (PubMed:17581814). {ECO:0000269|PubMed:11713244,
CC ECO:0000269|PubMed:17581814, ECO:0000269|PubMed:8569530}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11713244,
CC ECO:0000269|PubMed:17581814, ECO:0000269|PubMed:8569530}.
CC -!- MISCELLANEOUS: This protein can also be encoded on a prophage.
CC {ECO:0000305}.
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DR EMBL; AB037920; BAA90658.1; -; Genomic_DNA.
DR PDB; 2E4M; X-ray; 1.85 A; C=1-146.
DR PDBsum; 2E4M; -.
DR SMR; Q9LBR4; -.
DR UniLectin; Q9LBR4; -.
DR PATRIC; fig|1491.434.peg.24; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR008903; HA-17_C_botulinum.
DR InterPro; IPR035992; Ricin_B-like_lectins.
DR PIRSF; PIRSF037660; Botulinum_HA-17; 1.
DR SUPFAM; SSF50370; SSF50370; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Hemagglutinin; Secreted;
KW Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11713244,
FT ECO:0000269|PubMed:17581814, ECO:0000269|PubMed:8569530"
FT CHAIN 2..146
FT /note="Hemagglutinin component HA-17 type D"
FT /id="PRO_0000445710"
FT STRAND 10..19
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 21..27
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 41..43
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 45..49
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 55..60
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 63..70
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 74..80
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 87..93
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 105..107
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 109..114
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 126..131
FT /evidence="ECO:0007829|PDB:2E4M"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:2E4M"
FT STRAND 141..145
FT /evidence="ECO:0007829|PDB:2E4M"
SQ SEQUENCE 146 AA; 16705 MW; 0D3115E48B2AA6A7 CRC64;
MSSERTFLPN GNYKIKSLFS DSLYLTYSSG SLSFLNTSSL DNQKWKLEYI SSSNGFRFSN
VAEPNKYLAY NDYGFIYLSS SSNNSLWNPI KIAINSYIIC TLSIVNVTDY AWTIYDNNNN
ITDQPILNLP NFDINNSNQI LKLEKL
