GenomeNet

Database: UniProt
Entry: A9IND3_BORPD
LinkDB: A9IND3_BORPD
Original site: A9IND3_BORPD 
ID   A9IND3_BORPD            Unreviewed;       352 AA.
AC   A9IND3;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   24-JAN-2024, entry version 77.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   OrderedLocusNames=Bpet2479 {ECO:0000313|EMBL:CAP42821.1};
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42821.1, ECO:0000313|Proteomes:UP000001225};
RN   [1] {ECO:0000313|EMBL:CAP42821.1, ECO:0000313|Proteomes:UP000001225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC   {ECO:0000313|Proteomes:UP000001225};
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
CC   -!- FUNCTION: Extracellular zinc metalloprotease.
CC       {ECO:0000256|RuleBase:RU366073}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={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; AM902716; CAP42821.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9IND3; -.
DR   STRING; 94624.Bpet2479; -.
DR   MEROPS; M04.023; -.
DR   KEGG; bpt:Bpet2479; -.
DR   eggNOG; COG3227; Bacteria.
DR   OMA; FCTIVPP; -.
DR   Proteomes; UP000001225; 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; 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; 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   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU366073};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU366073};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU366073};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   DOMAIN          100..181
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          185..350
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          49..69
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..273
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        175
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        276
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   352 AA;  37703 MW;  0800F9590CF726E3 CRC64;
     MSRVMSDPWC SGVIPPYMLD RLTRHASPRV RQRALSTLRL EAQARSLRAT ATAAPAGTRA
     PATAVSPPGQ VSRAVHSATN GTVLPGLLVR AEGQPPSGDP AVDEAYEHLG ATYDMFWQVY
     RRHSIDNAGL PLVGTVHYGE DYDNAFWNGA QMVFGDGDGE VFNRFTVAVD IVGHELSHGV
     IDHEAGLRYQ GQSGALNESL SDVFGSLVKQ HRAGQTADQA DWLIGAGLFT SAVNARALRS
     MAQPGSAYDD PALGKDPQPA HMQDYVDTTD DNGGVHINSG IPNRAFYLAA TALGGPAWQR
     AGRVWYDALR DKRLGAQADF ASFATLTLEA ASADAATRQA VREAWRQVGV LP
//
DBGET integrated database retrieval system