HA70D_CBDP
ID HA70D_CBDP Reviewed; 623 AA.
AC Q9LBR5;
DT 07-NOV-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 29-SEP-2021, entry version 53.
DE RecName: Full=Hemagglutinin component HA-70 type D;
DE AltName: Full=HA3 {ECO:0000303|PubMed:8569530};
GN Name=ha-70 {ECO:0000303|PubMed:11713244}; Synonyms=ha70;
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; 13-24 AND
RP 190-199, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND PROTEOLYTIC CLEAVAGE.
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 7-20 AND 193-207, 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]
RP PROTEIN 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
CC (Probable). Erythrocyte agglutination only occurs when the entire
CC complex is assembled (PubMed:17581814). This HA subunit probably
CC connects toxin/NTNHA to HA-33 and HA-17, the other components of the HA
CC complex, and it may also protect the M toxin from proteolysis upon
CC secretion (PubMed:11713244). {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:17581814). M toxin consists of a non-toxic, non-hemagglutinin
CC component (NTNHA) and the neurotoxin (BoNT/D) (PubMed:11713244,
CC PubMed:8569530, PubMed:17581814). L toxin consists of the M toxin and
CC the 3 hemagglutinin (HA) subcomponents of 70, 33, and 17 kDa
CC (PubMed:8569530). The stoichiometry of the whole complex has been
CC modeled as one BoNT/D, one NTNHA, three HA-70, six HA-33 and three HA-
CC 17 (PubMed:17581814). HA-33 and HA-17 crystallize as a heterotrimer
CC with two HA-33 and one HA-17 (PubMed:17581814).
CC {ECO:0000269|PubMed:11713244, ECO:0000269|PubMed:17581814,
CC ECO:0000269|PubMed:8569530}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:11713244,
CC ECO:0000269|PubMed:17581814, ECO:0000269|PubMed:8569530}.
CC -!- PTM: Limited treatment of L toxin with pepsin or trypsin produces
CC shorter HA-70 proteins (called HA-55, HA-23 and HA-22) sometimes
CC observed in vivo in other strains of type C and D botulinum toxin
CC preparations. {ECO:0000269|PubMed:11713244}.
CC -!- MISCELLANEOUS: This protein can also be encoded on a prophage.
CC {ECO:0000305}.
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DR EMBL; AB037920; BAA90657.1; -; Genomic_DNA.
DR SMR; Q9LBR5; -.
DR PATRIC; fig|1491.434.peg.25; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR003897; Clenterotox.
DR InterPro; IPR040597; HA70_C.
DR Pfam; PF03505; Clenterotox; 2.
DR Pfam; PF17993; HA70_C; 1.
DR PRINTS; PR01394; CLENTEROTOXN.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Hemagglutinin; Secreted; Virulence.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:11713244,
FT ECO:0000269|PubMed:17581814"
FT CHAIN 2..623
FT /note="Hemagglutinin component HA-70 type D"
FT /id="PRO_0000445711"
FT CONFLICT 193
FT /note="D -> N (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..200
FT /note="TTNL -> NINF (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 623 AA; 70311 MW; DF4D7860466E48CE CRC64;
MSLSIKELYY TKDKSINNVN LADGNYVVNR GDGWILSRQN QNLGGNISNN GCTAIVGDLR
IRETATPYYY PTASFNEEYI RNNVQNVFAN FTEASEIPIG FEFSKTAPSN KGLYMYLQYT
YIRYEIIKVL RNTVIERAVL YVPSLGYAKS IEFNSGEQID KNFYFTSEDK CILNEKFIYK
KIAETTTAKE SNDSNNTTNL NTSQTILPYP NGLYVINKGD GYMRTNDKDL IGTLLIETNT
SGSIIQPRLR NTTRPLFNTS NPTLFSQEYT EARLNDAFNI QLFNTSTTLF KFVEEAPDNK
NISMKAYNTY EKYELINYQN GNIADKAEYY LPSLGKCEVS DAPSPQAPVV ETPVEQDGFI
QTGPNENIIV GVINPSENIE EISTPIPDDY TYNIPTSIQN NACYVLFTVN TTGVYKINAQ
NNLPPLIIYE SIGSDNMNIQ SNTLSNNNIK AINYITGTDS SNAESYLIVS LIKNKNYYIR
IPQISSSTTN QLIFKRELGN ISDLANSTVN ILDNLNTSGT HYYTRQSPDV GNYISYQLTI
PGDFNNIASS IFSFRTRNNQ GIGTLYRLTE SINGYNLITI KNYSDLLNNV EPISLLNGAT
YIFRVKVTEL NNYNIIFDAY RNS
