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Database: UniProt
Entry: N1NSR2_STRMB
LinkDB: N1NSR2_STRMB
Original site: N1NSR2_STRMB 
ID   N1NSR2_STRMB            Unreviewed;       518 AA.
AC   N1NSR2;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   08-NOV-2023, entry version 32.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   Name=mp1 {ECO:0000313|EMBL:CCW72535.1};
OS   Streptomyces mobaraensis (Streptoverticillium mobaraense).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=35621 {ECO:0000313|EMBL:CCW72535.1};
RN   [1] {ECO:0000313|EMBL:CCW72535.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 40847 {ECO:0000313|EMBL:CCW72535.1};
RA   Zindel S., Froels S., Kletzin A., Pfeifer F., Fuchsbauer H.L.;
RT   "Gene structures of the Transglutaminase-activating metalloprotease and two
RT   related putative metalloproteases from Streptomyces mobaraensis.";
RL   Submitted (APR-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}.
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DR   EMBL; HF968453; CCW72535.1; -; Genomic_DNA.
DR   AlphaFoldDB; N1NSR2; -.
DR   MEROPS; M04.017; -.
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   InterPro; IPR006311; TAT_signal.
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.
DR   PROSITE; PS51318; TAT; 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   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU366073};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU366073}.
FT   SIGNAL          1..40
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           41..518
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023156299"
FT   DOMAIN          58..105
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          197..345
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          348..517
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        338
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        420
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   518 AA;  55269 MW;  8D14378698DCDD45 CRC64;
     MRHTPRIARS GSRRPAVAAS AATVAAALLA SGFAGAPAQA AGQEDPAKAL HLSGKERLVP
     RGTVTDEDGT VHTRYERTYE GLPVLGGDLV VHQDKQGKVE DVTKAVEAAI KVPTTKAKIS
     APAARRQAML ASADEGAGAF ISNQAPRKVV WAAKGTPVLA YETVVGGLQH DGTPSELHVV
     TDATTGKKLD EFQAIATGTG TGMYNGKVPV NSVKSGGRFY MKDGQRGGHT TFHAQNKKSG
     ESFPAFSNTR DVWGNGKQSM AQTAAVDAQY GAAMTWDYYK NVLGRKGIKG NGKAANSFVH
     YGNGYNNAFW SDECFCMVYG DGKGNKAPLT SLDVAGHEMT HGVTSATARL RYEGESGGLN
     EATSDIFGTA VEFYARNGQD KGDYLIGEKL GKPLRYMDKP SKDGRSADYW RKDLGDLDVH
     YSSGVANHFF YLLAEGSGAK TINGVKYNSP TWGGIKVNGI GRGAAEKLWY KALTVYMTTN
     TDYKGARSAT LKAARDMFGT KSKQYKTVQA AWDGVNVK
//
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