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Database: UniProt
Entry: A0A0A0JR96_9MICO
LinkDB: A0A0A0JR96_9MICO
Original site: A0A0A0JR96_9MICO 
ID   A0A0A0JR96_9MICO        Unreviewed;       538 AA.
AC   A0A0A0JR96;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=N803_07300 {ECO:0000313|EMBL:KGN38542.1};
OS   Knoellia subterranea KCTC 19937.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Intrasporangiaceae;
OC   Knoellia.
OX   NCBI_TaxID=1385521 {ECO:0000313|EMBL:KGN38542.1, ECO:0000313|Proteomes:UP000030011};
RN   [1] {ECO:0000313|EMBL:KGN38542.1, ECO:0000313|Proteomes:UP000030011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 19937 {ECO:0000313|EMBL:KGN38542.1,
RC   ECO:0000313|Proteomes:UP000030011};
RA   Zhu W., Wang G.;
RT   "The genome sequence of Knoellia subterranea.";
RL   Submitted (AUG-2013) 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:KGN38542.1}.
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DR   EMBL; AVPK01000002; KGN38542.1; -; Genomic_DNA.
DR   RefSeq; WP_035902925.1; NZ_AVPK01000002.1.
DR   AlphaFoldDB; A0A0A0JR96; -.
DR   STRING; 1385521.N803_07300; -.
DR   MEROPS; M04.017; -.
DR   eggNOG; COG3227; Bacteria.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000030011; 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; 3.10.450.490; -; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR011096; FTP_domain.
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; PTHR33794; BACILLOLYSIN; 1.
DR   PANTHER; PTHR33794:SF1; BACILLOLYSIN; 1.
DR   Pfam; PF07504; FTP; 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:UP000030011};
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..19
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           20..538
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5039744231"
FT   DOMAIN          77..114
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          205..361
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          364..537
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        354
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        440
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   538 AA;  55710 MW;  3343AA5CFAE8FD64 CRC64;
     MRRSLSVLAC LAAGSAAIAT VVPAASARPA DPIGPLRQLD VASVGASAEQ ALRAAPGLLR
     LAAGEDLIAS SALGESSGAR HVRMNRTYAG LPVLGGDLVA HLGADGAVDS VSQTLRAPLT
     VSTTPKITSA KARQATRPTL PAGVNLDKAA PTLAVDATDG TPRLVWDVRA SGVRENGTPS
     RLHTWVDATT GAVVGSADEI HEADGSGSSL YSGTVTIQTT QSGSSYQLKD TTRGNSQVTD
     MGNKTDSIFC QILQIGCSAG TLYTDADNVW GTGSNFNRQT AAVDAAYGQA RTWDYFKNAH
     GRNGIWNTGQ GSPSRVHYGS NYVNAFWDGK QMTYGDGDGS SFGPLVSLDV AGHEMSHGVI
     ENSANLTYSK ESGGLNESTS DIFGTMVEFS ANNPNDPGDY LIGEEFDLAK GLGFRRMDNP
     SSDGSSVNCW SSSVANLDVH YSSGVGNHFF YLLAEGSGAK TFGGKAHNST TCNGTTISGI
     GRDAAAKIWY RALTVYMTSS TNYSGARAAT VKAAGDLYGA SSTQAAAVAK AWDAVSVK
//
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