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
//