ID B1IKP9_CLOBK Unreviewed; 592 AA.
AC B1IKP9;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN Name=npr {ECO:0000313|EMBL:ACA45922.1};
GN OrderedLocusNames=CLD_3107 {ECO:0000313|EMBL:ACA45922.1};
OS Clostridium botulinum (strain Okra / Type B1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498213 {ECO:0000313|EMBL:ACA45922.1, ECO:0000313|Proteomes:UP000008541};
RN [1] {ECO:0000313|EMBL:ACA45922.1, ECO:0000313|Proteomes:UP000008541}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Okra / Type B1 {ECO:0000313|Proteomes:UP000008541};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
CC -!- FUNCTION: Extracellular zinc metalloprotease.
CC {ECO:0000256|RuleBase:RU366073}.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947,
CC ECO:0000256|RuleBase:RU366073};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|RuleBase:RU366073}.
CC -!- SIMILARITY: Belongs to the peptidase M4 family.
CC {ECO:0000256|ARBA:ARBA00009388, ECO:0000256|RuleBase:RU366073}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000939; ACA45922.1; -; Genomic_DNA.
DR RefSeq; WP_003405778.1; NC_010516.1.
DR AlphaFoldDB; B1IKP9; -.
DR KEGG; cbb:CLD_3107; -.
DR HOGENOM; CLU_008590_5_2_9; -.
DR Proteomes; UP000008541; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd09597; M4_TLP; 1.
DR Gene3D; 3.10.170.10; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR InterPro; IPR011096; FTP_domain.
DR InterPro; IPR025711; PepSY.
DR InterPro; IPR023612; Peptidase_M4.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR InterPro; IPR001570; Peptidase_M4_C_domain.
DR InterPro; IPR013856; Peptidase_M4_domain.
DR PANTHER; PTHR43579; -; 1.
DR PANTHER; PTHR43579:SF1; NEUTRAL METALLOPROTEINASE; 1.
DR Pfam; PF07504; FTP; 1.
DR Pfam; PF03413; PepSY; 1.
DR Pfam; PF01447; Peptidase_M4; 1.
DR Pfam; PF02868; Peptidase_M4_C; 1.
DR PRINTS; PR00730; THERMOLYSIN.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW Metalloprotease {ECO:0000256|RuleBase:RU366073};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW Secreted {ECO:0000256|RuleBase:RU366073};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT CHAIN 22..592
FT /note="Neutral metalloproteinase"
FT /evidence="ECO:0000256|RuleBase:RU366073"
FT /id="PRO_5039755727"
FT DOMAIN 85..133
FT /note="FTP"
FT /evidence="ECO:0000259|Pfam:PF07504"
FT DOMAIN 148..211
FT /note="PepSY"
FT /evidence="ECO:0000259|Pfam:PF03413"
FT DOMAIN 263..430
FT /note="Peptidase M4"
FT /evidence="ECO:0000259|Pfam:PF01447"
FT DOMAIN 433..584
FT /note="Peptidase M4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02868"
FT COILED 220..250
FT /evidence="ECO:0000256|SAM:Coils"
FT ACT_SITE 423
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT ACT_SITE 503
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ SEQUENCE 592 AA; 66201 MW; D732597234F031BE CRC64;
MKSKKLLATV LSAVITFSAV SAVSAAPVGK ESKSEPKITT ISWDKSEQNT KKAATDIKQK
KFNNAQEVTN FFEKNISKFG VKKGTLKSTK TLKDDKGKTH YHTIYEVEGI PVYYGRIVFT
TEKDSTMNSI NGRVDTVFEN GNWKNKIKLS KEEAIAKAKG DIKDQKSNSE KADLYLYNFE
GNPYVVYLVN ATTDNGNWNV FVNAEDGSIV NKFDTTPTLV ENKDKKLPNA KKIKDEAEKN
EAKKANASNV NSVTDVQGQS VKGIGRTSLD GLVNIDLTYG NGKYYLKDNN RKIYLYDLKN
QVSGDDLYRY IIEHYYYGAP DYKQRLMSQS ELVSNSNNNF INDNQVNSVD AYVNTAKTYD
YYKNKLSRNS IDNKGMNVNG FVHVDKNLGN AFWYGPYDSM FFGDGDGVRF SALAKSLDVV
GHELSHGVTN KQSDLNYENE SGALNESFSD IMGTAVEGKN FVLGEDCWIA GGVMRDMENP
SRGNQPAHMK DYAYMSEDNG GVHKNSGIIN HAAYLIADGF EKMGTKDSKD IMGKLFYIAN
CYYWDQTTDF AKCRNDVVRV AKDLYGDNSK EVEIVKNAFD KVGVYATPQL SL
//
