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Database: UniProt
Entry: A0A1Z2L2M2_9ACTN
LinkDB: A0A1Z2L2M2_9ACTN
Original site: A0A1Z2L2M2_9ACTN 
ID   A0A1Z2L2M2_9ACTN        Unreviewed;       538 AA.
AC   A0A1Z2L2M2;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=SMD11_2868 {ECO:0000313|EMBL:ARZ68516.1};
OS   Streptomyces albireticuli.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ68516.1, ECO:0000313|Proteomes:UP000195755};
RN   [1] {ECO:0000313|EMBL:ARZ68516.1, ECO:0000313|Proteomes:UP000195755}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ68516.1,
RC   ECO:0000313|Proteomes:UP000195755};
RA   Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT   "Streptomyces albireticuli Genome sequencing and assembly.";
RL   Submitted (JUN-2017) 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; CP021744; ARZ68516.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z2L2M2; -.
DR   KEGG; salj:SMD11_2868; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000195755; 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; 3.10.450.40; -; 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   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..36
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           37..538
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5039747626"
FT   DOMAIN          79..120
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          217..360
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          363..537
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        353
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;  56310 MW;  BAF18D07B2DFEA3A CRC64;
     MRSITSTSRK NTLRAAALVA SAAMVVVGVQ SGAANASADR ATGAQQLTLS ADQRVAAIKG
     AQTDAASTAA KIGLGGKEKL VVRDVIKDAD GTVHTRYERT FDGLPVLGGD LVVHEAKGGK
     RSVDKATEAD IAVPTTTPSL APSAAKKSAL SAAAEEKTAK ADTQSPRKVV WAASGKPVLA
     YETVVTGVQK DGTPSKLHVI TDAATGKKLF QREGVHTGTG TSTYSGKVNL TTTKSGSTFQ
     LNDSARGGHK TYDLNQGSSG TGTIYTDADD VWGGGRQTAG VDAHYGAATT WDFYKNVLGR
     SGIKNDGKGA YSRVHYGNGY VNAFWDDECF CMTYGDGENN ANPLTALDVA AHEMTHGVTS
     ATANLNYSGE SGGLNEATSD IFGTATEFFA NNSSDTGDYL IGEEININGD GTPLRYMDKP
     SKDGASKDYW SSGLGNTDVH YSSGPANHFF YLLSEGSGAK TINGVSYNSP TYNNSKITGI
     GRDKATKIWY KALTTYFTST TNYKAARAGT LKATADLYGS TSTEYKTVAA AWTAINVK
//
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