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Database: UniProt
Entry: K9ANN2_9MICO
LinkDB: K9ANN2_9MICO
Original site: K9ANN2_9MICO 
ID   K9ANN2_9MICO            Unreviewed;       364 AA.
AC   K9ANN2;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=C272_04950 {ECO:0000313|EMBL:EKU48879.1};
OS   Brevibacterium casei S18.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC   Brevibacterium.
OX   NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU48879.1, ECO:0000313|Proteomes:UP000009879};
RN   [1] {ECO:0000313|EMBL:EKU48879.1, ECO:0000313|Proteomes:UP000009879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S18 {ECO:0000313|EMBL:EKU48879.1,
RC   ECO:0000313|Proteomes:UP000009879};
RA   Sharma R., Singh A., Jangir P.K.;
RT   "Genome Sequence of Brevibacterium casei S18.";
RL   Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EKU48879.1}.
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DR   EMBL; AMSP01000002; EKU48879.1; -; Genomic_DNA.
DR   AlphaFoldDB; K9ANN2; -.
DR   MEROPS; M04.023; -.
DR   PATRIC; fig|1229781.4.peg.994; -.
DR   eggNOG; COG3227; Bacteria.
DR   Proteomes; UP000009879; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000009879};
KW   Secreted {ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   DOMAIN          72..177
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          181..350
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          41..78
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        51..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        171
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        272
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   364 AA;  38157 MW;  D1C7DF79C15477BE CRC64;
     MVPPYLLSNL ADNGGERFPR AADAARTGLR ADARVRQLRA EGLRAAPDGS SATARTRSAQ
     AGEATGPNRQ IHDAQNKEDL PGVLVRSEGE EPVADDAVNE AYDGLGASYA LFAEAFDRNS
     LDGQGGPLLA SVHYGQDYDN AFWDGRLLVF GDGDGEVFTG FTGSLSIIGH ELSHGVITHT
     ADLEYFDQSG ALNEHCADVF GALTEQHSAG QNAEDATWLI GAGIFTEAVT GKALRSMIAP
     GTAYDDDVLG KDPQPDHMDG FVRTESDNGG VHLNSGIPNR AFAVAATTVG GPAWETVGQV
     WYGVLTGSEI TTTTDFAQFA DLTIAEAADQ FGEGSDVHDA VVEGWTTVGV VTGPAARGNR
     GSSW
//
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