BXAN_CLOBO
ID BXAN_CLOBO Reviewed; 1193 AA.
AC Q45914;
DT 18-JUL-2018, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Non-toxic nonhemagglutinin type A;
DE Short=NTNHA;
DE AltName: Full=Botulinum neurotoxin type A non-toxic component;
GN Name=ant; Synonyms=ntnh; ORFNames=ACP52_06665;
OS Clostridium botulinum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1491;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NIH / Type A;
RX PubMed=8521962; DOI=10.1016/0014-5793(95)01241-5;
RA Fujita R., Fujinaga Y., Inoue K., Nakajima H., Kumon H., Oguma K.;
RT "Molecular characterization of two forms of nontoxic-nonhemagglutinin
RT components of Clostridium botulinum type A progenitor toxins.";
RL FEBS Lett. 376:41-44(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17862 / Type A;
RG Consortium for Microbial Forensics and Genomics (microFORGE);
RA Knight B.M., O'Shea R.M., Jones B.A., Roberts D.P., Lin D., Hari K.,
RA Winegar R.A.;
RT "Draft genome sequence of Clostridium botulinum strain ATCC 17862.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0007744|PDB:3V0A, ECO:0007744|PDB:3V0B}
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH BONT/A, FUNCTION,
RP SUBUNIT, DOMAIN, PROTEOLYTIC CLEAVAGE, AND DISULFIDE BONDS.
RC STRAIN=Type A;
RX PubMed=22363010; DOI=10.1126/science.1214270;
RA Gu S., Rumpel S., Zhou J., Strotmeier J., Bigalke H., Perry K.,
RA Shoemaker C.B., Rummel A., Jin R.;
RT "Botulinum neurotoxin is shielded by NTNHA in an interlocked complex.";
RL Science 335:977-981(2012).
CC -!- FUNCTION: Assembles with botulinum neurotoxin type A (BoNT/A) 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 (PubMed:22363010). Necessary for neurotoxicity.
CC {ECO:0000269|PubMed:22363010}.
CC -!- SUBUNIT: Forms a highly interlocked heterodimer with botulinum
CC neurotoxin type A at pH 6.0 but not at pH 7.5, called the minimally
CC functional progenitor toxin complex (M-PTC) (BoNT/A, botA)
CC (PubMed:22363010).
CC -!- INTERACTION:
CC Q45914; A5HZZ4: ha70; Xeno; NbExp=5; IntAct=EBI-16109965, EBI-16109901;
CC -!- DOMAIN: Has 3 domains that are structurally very similar to those in
CC BoNT/A; light chain (nLC, equivalent to the light chain, residues 1-
CC 408), N-heavy chain (nHN, residues 409-829) and C-heavy chain (nHC,
CC residues 830-1193) (PubMed:22363010). {ECO:0000269|PubMed:22363010}.
CC -!- PTM: The 133-Lys-|-Lys-134 bond is cleaved during long-term storage;
CC the cleavage site is masked in the M-PTC complex (PubMed:22363010).
CC {ECO:0000269|PubMed:22363010}.
CC -!- SIMILARITY: Belongs to the botulism non-toxic nonhemagglutinin family.
CC {ECO:0000305}.
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DR EMBL; D67030; BAA11050.1; -; Genomic_DNA.
DR EMBL; LGIK01000019; KON10585.1; -; Genomic_DNA.
DR PIR; S68218; S68218.
DR RefSeq; WP_011948510.1; NZ_LHUL01000004.1.
DR PDB; 3V0A; X-ray; 2.70 A; B=1-1193.
DR PDB; 3V0B; X-ray; 3.90 A; B=1-1193.
DR PDBsum; 3V0A; -.
DR PDBsum; 3V0B; -.
DR AlphaFoldDB; Q45914; -.
DR SMR; Q45914; -.
DR DIP; DIP-1006N; -.
DR IntAct; Q45914; 1.
DR EnsemblBacteria; KON10585; KON10585; ACP52_06665.
DR GeneID; 5185060; -.
DR PATRIC; fig|1491.444.peg.1066; -.
DR OMA; GWEIYFE; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
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 3D-structure; Disulfide bond; Virulence.
FT CHAIN 1..1193
FT /note="Non-toxic nonhemagglutinin type A"
FT /id="PRO_0000444923"
FT REGION 1..408
FT /note="Light chain nLC"
FT /evidence="ECO:0000269|PubMed:22363010"
FT REGION 409..829
FT /note="N-heavy chain nHN"
FT /evidence="ECO:0000269|PubMed:22363010"
FT REGION 830..1193
FT /note="C-heavy chain nHC; required for protection of BoNT/A
FT at pH 2.0"
FT /evidence="ECO:0000269|PubMed:22363010"
FT SITE 133..134
FT /note="Cleaved during long-term storage, protected in M-PTC
FT complex"
FT /evidence="ECO:0000269|PubMed:22363010"
FT DISULFID 583..755
FT /evidence="ECO:0007744|PDB:3V0A, ECO:0007744|PDB:3V0B"
FT STRAND 15..22
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 29..36
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3V0A"
FT TURN 66..69
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 72..90
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 93..104
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 155..158
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 182..186
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 188..192
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 193..195
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 199..202
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 218..234
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 243..248
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 257..261
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 262..268
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 273..276
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 286..304
FT /evidence="ECO:0007829|PDB:3V0A"
FT TURN 305..308
FT /evidence="ECO:0007829|PDB:3V0A"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 314..323
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 328..333
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 336..342
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 355..358
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:3V0A"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 390..394
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 400..406
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 412..418
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 430..433
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 459..463
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 500..505
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 515..518
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 520..524
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 531..533
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 537..545
FT /evidence="ECO:0007829|PDB:3V0A"
FT TURN 546..548
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 555..573
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 576..581
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 584..589
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 592..596
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 601..603
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 605..612
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 614..617
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 643..675
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 677..711
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 717..759
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 761..785
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 788..790
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 792..801
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 806..809
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 814..819
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 824..833
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 834..845
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 848..853
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 860..863
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 868..871
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 873..880
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 882..884
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 887..890
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 892..895
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 902..910
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 918..925
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 928..935
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 938..944
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 950..955
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 960..962
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 964..971
FT /evidence="ECO:0007829|PDB:3V0A"
FT TURN 972..975
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 976..981
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 984..990
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1001..1005
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1012..1022
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 1026..1037
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1039..1041
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1047..1049
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1055..1063
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1067..1081
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1094..1097
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1111..1126
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1130..1136
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 1138..1140
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1144..1147
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1156..1160
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1163..1170
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1175..1179
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1181..1183
FT /evidence="ECO:0007829|PDB:3V0A"
FT HELIX 1185..1188
FT /evidence="ECO:0007829|PDB:3V0A"
FT STRAND 1190..1193
FT /evidence="ECO:0007829|PDB:3V0A"
SQ SEQUENCE 1193 AA; 138093 MW; 9052B13E6E0F9848 CRC64;
MNINDNLSIN SPVDNKNVVV VRARKTDTVF KAFKVAPNIW VAPERYYGES LSIDEEYKVD
GGIYDSNFLS QDSEKDKFLQ AIITLLKRIN STNAGEKLLS LISTAIPFPY GYIGGGYYAP
NMITFGSAPK SNKKLNSLIS STIPFPYAGY RETNYLSSED NKSFYASNIV IFGPGANIVE
NNTVFYKKED AENGMGTMTE IWFQPFLTYK YDEFYIDPAI ELIKCLIKSL YFLYGIKPSD
DLVIPYRLRS ELENIEYSQL NIVDLLVSGG IDPKFINTDP YWFTDNYFSN AKKVFEDHRN
IYETEIEGNN AIGNDIKLRL KQKFRININD IWELNLNYFS KEFSIMMPDR FNNALKHFYR
KQYYKIDYPE NYSINGFVNG QINAQLSLSD RNQDIINKPE EIINLLNGNN VSLMRSNIYG
DGLKSTVDDF YSNYKIPYNR AYEYHFNNSN DSSLDNVNIG VIDNIPEIID VNPYKENCDK
FSPVQKITST REINTNIPWP INYLQAQNTN NEKFSLSSDF VEVVSSKDKS LVYSFLSNVM
FYLDSIKDNS PIDTDKKYYL WLREIFRNYS FDITATQEIN TNCGINKVVT WFGKALNILN
TSDSFVEEFQ NLGAISLINK KENLSMPIIE SYEIPNDMLG LPLNDLNEKL FNIYSKNTAY
FKKIYYNFLD QWWTQYYSQY FDLICMAKRS VLAQETLIKR IIQKKLSYLI GNSNISSDNL
ALMNLTTTNT LRDISNESQI AMNNVDSFLN NAAICVFESN IYPKFISFME QCINNINIKT
KEFIQKCTNI NEDEKLQLIN QNVFNSLDFE FLNIQNMKSL FSSETALLIK EETWPYELVL
YAFKEPGNNV IGDASGKNTS IEYSKDIGLV YGINSDALYL NGSNQSISFS NDFFENGLTN
SFSIYFWLRN LGKDTIKSKL IGSKEDNCGW EIYFQDTGLV FNMIDSNGNE KNIYLSDVSN
NSWHYITISV DRLKEQLLIF IDDNLVANES IKEILNIYSS NIISLLSENN PSYIEGLTIL
NKPTTSQEVL SNYFEVLNNS YIRDSNEERL EYNKTYQLYN YVFSDKPICE VKQNNNIYLT
INNTNNLNLQ ASKFKLLSIN PNKQYVQKLD EVIISVLDNM EKYIDISEDN RLQLIDNKNN
AKKMIISNDI FISNCLTLSY NGKYICLSMK DENHNWMICN NDMSKYLYLW SFK
