ID   BXCN_CBCP               Reviewed;        1196 AA.
AC   P46081;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 84.
DE   RecName: Full=Non-toxic nonhemagglutinin type C;
DE            Short=NTNHA;
DE   AltName: Full=ANTP139;
DE   AltName: Full=Botulinum neurotoxin type C non-toxic component;
DE   AltName: Full=Botulinum neurotoxin type C1 non-toxic component;
OS   Clostridium botulinum C phage (Clostridium botulinum C bacteriophage).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Caudovirales; Siphoviridae.
OX   NCBI_TaxID=12336;
OH   NCBI_TaxID=36828; Clostridium botulinum C.
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Stockholm / Type C;
RX   PubMed=1567404; DOI=10.1016/s0006-291x(05)80328-6;
RA   Tsuzuki K., Kimura K., Fujii N., Yokosawa N., Oguma K.;
RT   "The complete nucleotide sequence of the gene coding for the nontoxic-
RT   nonhemagglutinin component of Clostridium botulinum type C progenitor
RT   toxin.";
RL   Biochem. Biophys. Res. Commun. 183:1273-1279(1992).
RN   [2]
RP   SUBUNIT, AND SUBCELLULAR LOCATION.
RC   STRAIN=Stockholm / Type C / phage C-ST;
RX   PubMed=7802661; DOI=10.1006/bbrc.1994.2805;
RA   Fujinaga Y., Inoue K., Shimazaki S., Tomochika K., Tsuzuki K., Fujii N.,
RA   Watanabe T., Ohyama T., Takeshi K., Inoue K., Oguma K.;
RT   "Molecular construction of Clostridium botulinum type C progenitor toxin
RT   and its gene organization.";
RL   Biochem. Biophys. Res. Commun. 205:1291-1298(1994).
CC   -!- FUNCTION: Assembles with botulinum neurotoxin type C (BoNT/C) and
CC       protects it against pH-mediated inactivation or protease activity at pH
CC       2.6 (the pH of the animal gastrointestinal tract) but not at pH 6.0.
CC       The non-toxic component is necessary to maintain toxicity.
CC       {ECO:0000250|UniProtKB:Q45914}.
CC   -!- SUBUNIT: Forms a highly interlocked heterodimer with botulinum
CC       neurotoxin type C at pH 6.0 but not at pH 7.5 (By similarity).
CC       Botulinum toxins are produced as progenitor toxins of large molecular
CC       sizes of 12S (M toxin) and 16S (L toxin). M toxin consists of a non-
CC       toxic, non-hemagglutinin component (NTNHA) and the neurotoxin
CC       (Probable). L toxin consists of the M toxin and the 3 subcomponents of
CC       hemagglutinin (HA) (PubMed:7802661). HA is composed of subcomponents of
CC       70, 33, and 17 kDa (PubMed:7802661). The 70 kDa subcomponent undergoes
CC       proteolytic processing and is split into HA-55 and HA-22-23
CC       (PubMed:7802661). The stoichiometry of the whole complex has been
CC       modeled as one BoNT/C, one NTNHA, three HA-70, six HA-33 and three HA-
CC       17 (By similarity). {ECO:0000250|UniProtKB:Q45914,
CC       ECO:0000250|UniProtKB:Q9LBR2, ECO:0000269|PubMed:7802661,
CC       ECO:0000305|PubMed:7802661}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7802661}.
CC   -!- DOMAIN: Has 3 domains that are structurally very similar to those in
CC       BoNT/C; light chain (nLC, equivalent to the light chain), N-heavy chain
CC       (nHN) and C-heavy chain (nHC). {ECO:0000250|UniProtKB:Q9LBR2}.
CC   -!- MISCELLANEOUS: This protein can also be encoded on a prophage.
CC       {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the botulism non-toxic nonhemagglutinin family.
CC       {ECO:0000305}.
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DR   EMBL; X62389; CAA44262.1; -; Genomic_DNA.
DR   RefSeq; YP_398515.1; NC_007581.1.
DR   SMR; P46081; -.
DR   TCDB; 1.C.8.1.4; the botulinum and tetanus toxin (btt) family.
DR   PRIDE; P46081; -.
DR   GeneID; 3772940; -.
DR   KEGG; vg:3772940; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0046929; P:negative regulation of neurotransmitter secretion; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 1.20.1120.10; -; 1.
DR   InterPro; IPR000395; Bot/tetX_LC.
DR   InterPro; IPR036248; Clostridium_toxin_transloc.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR013677; Nontoxic_nonhemagglutn_C.
DR   InterPro; IPR012928; Toxin_rcpt-bd_N.
DR   Pfam; PF08470; NTNH_C; 1.
DR   Pfam; PF01742; Peptidase_M27; 1.
DR   Pfam; PF07953; Toxin_R_bind_N; 1.
DR   PRINTS; PR00760; BONTOXILYSIN.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF58091; SSF58091; 1.
PE   1: Evidence at protein level;
KW   Secreted; Virulence.
FT   CHAIN           1..1196
FT                   /note="Non-toxic nonhemagglutinin type C"
FT                   /id="PRO_0000065028"
FT   REGION          1..408
FT                   /note="Light chain nLC"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LBR2"
FT   REGION          409..828
FT                   /note="N-heavy chain nHN"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LBR2"
FT   REGION          829..1195
FT                   /note="C-heavy chain nHC"
FT                   /evidence="ECO:0000250|UniProtKB:Q9LBR2"
SQ   SEQUENCE   1196 AA;  138741 MW;  4BD5956274D7F9C3 CRC64;
     MDINDDLNIN SPVDNKNVVI VRARKTNTFF KAFKVAPNIW VAPERYYGEP LDIAEEYKLD
     GGIYDSNFLS QDSERENFLQ AIIILLKRIN NTISGKQLLS LISTAIPFPY GYIGGGYSSP
     NIFTFGKTPK SNKKLNSLVT STIPFPFGGY RETNYIESQN NKNFYASNII IFGPGSNIVE
     NNVIYYKKND AENGMGTMAE IVFQPLLTYK YNKFYIDPAM ELTKCLIKSL YFLYGIKPSD
     NLVVPYRLRT ELDNKQFSQL NIIDLLISGG VDLEFINTNP YWFTNSYFPN SIKMFEKYKN
     IYKTEIEGNN AIGNDIKLRL KQKFQINVQD IWNLNLNYFC QSFNSIIPDR FSNALKHFYR
     KQYYTMDYTD NYNINGFVNG QINTKLPLSN KNTNIISKPE KVVNLVNENN ISLMKSNIYG
     DGLKGTTEDF YSTYKIPYNE EYEYRFNDSD NFPLNNISIE EVDSIPEIID INPYKDNSDN
     LVFTQITSMT EEVTTHTALS INYLQAQITN NENFTLSSDF SKVVSSKDKS LVYSFLDNLM
     SYLETIKNDG PIDTDKKYYL WLKEVFKNYS FDINLTQEID SMCGINEVVL WFGKALNILN
     TSNSFVEEYQ DSGAISLISK KDNLREPNIE IDDISDSLLG LSFKDLNNKL YEIYSKNIVY
     FKKIYFSFLD QWWTEYYSQY FELICMAKQS ILAQESLVKQ IVQNKFTDLS KASIPPDTLK
     LIRETTEKTF IDLSNESQIS MNRVDNFLNK ASICVFVEDI YPKFISYMEK YINNINIKTR
     EFIQRCTNIN DNEKSILINS YTFKTIDFKF LDIQSIKNFF NSQVEQVMKE ILSPYQLLLF
     ASKGPNSNII EDISGKNTLI QYTESIELVY GVNGESLYLK SPNETIKFSN KFFTNGLTNN
     FTICFWLRFT GKNDDKTRLI GNKVNNCGWE IYFEDNGLVF EIIDSNGNQE SVYLSNIIND
     NWYYISISVD RLKDQLLIFI NDKNVANVSI DQILSIYSTN IISLVNKNNS IYVEELSVLD
     NPITSEEVIR NYFSYLDNSY IRDSSKSLLE YNKNYQLYNY VFPETSLYEV NDNNKSYLSL
     KNTDGINISS VKFKLINIDE SKVYVQKWDE CIICVLDGTE KYLDISPENN RIQLVSSKDN
     AKKITVNTDL FRPDCITFSY NDKYFSLSLR DGDYNWMICN DNNKVPKGAH LWILES