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
//