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Database: UniProt
Entry: A0A066Z093_9ACTN
LinkDB: A0A066Z093_9ACTN
Original site: A0A066Z093_9ACTN 
ID   A0A066Z093_9ACTN        Unreviewed;       550 AA.
AC   A0A066Z093;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=Neutral metalloproteinase {ECO:0000256|RuleBase:RU366073};
DE            EC=3.4.24.- {ECO:0000256|RuleBase:RU366073};
GN   ORFNames=KCH_50820 {ECO:0000313|EMBL:KDN83600.1};
OS   Kitasatospora cheerisanensis KCTC 2395.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN83600.1, ECO:0000313|Proteomes:UP000027178};
RN   [1] {ECO:0000313|EMBL:KDN83600.1, ECO:0000313|Proteomes:UP000027178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN83600.1,
RC   ECO:0000313|Proteomes:UP000027178};
RA   Nam D.H.;
RT   "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL   Submitted (MAY-2014) 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:KDN83600.1}.
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DR   EMBL; JNBY01000095; KDN83600.1; -; Genomic_DNA.
DR   RefSeq; WP_035866266.1; NZ_KK853997.1.
DR   AlphaFoldDB; A0A066Z093; -.
DR   MEROPS; M04.017; -.
DR   PATRIC; fig|1348663.4.peg.4918; -.
DR   eggNOG; COG3227; Bacteria.
DR   HOGENOM; CLU_008590_5_1_11; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000027178; 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; 3.10.450.40; -; 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   Reference proteome {ECO:0000313|Proteomes:UP000027178};
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..30
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT   CHAIN           31..550
FT                   /note="Neutral metalloproteinase"
FT                   /evidence="ECO:0000256|RuleBase:RU366073"
FT                   /id="PRO_5023037248"
FT   DOMAIN          70..114
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          225..372
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          375..549
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        365
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        452
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   550 AA;  56438 MW;  DB3A5770A7C81712 CRC64;
     MKRKLAVGAV LSASALLAGA IQVSAGIAQA APNPAAAQNS AGQHRGELLA LAAAQAPSAA
     KALGLGAQEK LVVKDAIVDA DGTRHLRYER TYDGLPVLGG DLVVHQDAKG KVKSSDKAVA
     GTLAPASLSP KLTAAQAASK ATGAVQSTVG ISKDADEAAL TSVTGASGNA ELVIWAADGA
     PRLAYRTTVE GMRADGTPSR QLLVTDADSG AVLSAHEEVQ TANATGTGNG VFVGSVSLTT
     TLSGSTYTLK DATRGGQYTS TLAGKTSGKG TVYSKTTNTW GSGAASNGES AAVDAQYGAA
     VTWDFYKNTF GRSGIRNDGV GAYSRVHYGS NYVNAFWDDS CFCMTYGDGS GNTHPLTELD
     VSGHEMSHGV TSNTAGLNYS GESGGLNEAT SDIFGSMVEF YANLSKDVPD YLIGELININ
     GNGTPLRYMD KPSKDGASAD YWSSTVGNKD VHYSSGVANH FFYLLAEGSG AKTINGVSYN
     SPTYNGAAVT GIGRAQATQI WYRALTVYMT STTNYKAART ATLNAAKDLY GSGSTQYNAV
     AAAWTGVNVS
//
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