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Database: UniProt
Entry: A0A066YVN0_9ACTN
LinkDB: A0A066YVN0_9ACTN
Original site: A0A066YVN0_9ACTN 
ID   A0A066YVN0_9ACTN        Unreviewed;       726 AA.
AC   A0A066YVN0;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Zinc metalloprotease {ECO:0000313|EMBL:KDN81995.1};
GN   ORFNames=KCH_61490 {ECO:0000313|EMBL:KDN81995.1};
OS   Kitasatospora cheerisanensis KCTC 2395.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN81995.1, ECO:0000313|Proteomes:UP000027178};
RN   [1] {ECO:0000313|EMBL:KDN81995.1, ECO:0000313|Proteomes:UP000027178}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN81995.1,
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   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388}.
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:KDN81995.1}.
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DR   EMBL; JNBY01000126; KDN81995.1; -; Genomic_DNA.
DR   RefSeq; WP_035867780.1; NZ_KK853997.1.
DR   AlphaFoldDB; A0A066YVN0; -.
DR   MEROPS; M04.017; -.
DR   PATRIC; fig|1348663.4.peg.5950; -.
DR   eggNOG; COG3227; Bacteria.
DR   HOGENOM; CLU_008590_5_1_11; -.
DR   OrthoDB; 291295at2; -.
DR   Proteomes; UP000027178; Unassembled WGS sequence.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
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; 2.60.120.260; Galactose-binding domain-like; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
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; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:KDN81995.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:KDN81995.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027178};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           24..726
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038366751"
FT   DOMAIN          76..116
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          217..369
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          373..545
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   REGION          254..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          550..608
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        554..576
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        577..608
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        363
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        448
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   726 AA;  75023 MW;  E44815CA71AED281 CRC64;
     MSRKNALAAA VAAALTLGTV TVAATQSTAA ASGSSARPGA GFRAMTADAR GEAIRTADRE
     AAAVARSLGL GADERLVAKD VLFDTDGARH VRYDRTYRGL PVIGGDLVVH YGKDGRSTGS
     DQAHQGAIRM AGTAPKLTAA DASAAAVKHA KHVKNARTDS SDSSALVVYA VGKVPVLAYR
     STVTGEGETG PASREAVIVD AASGAPLDQY ELHQGITGTG NGVTVGQVSI ETTQSGSGYT
     LTDAAHGSTV VYDSYNSPQS NPKQNARTFS KTTNTWGTGT TSSRESAAVD ASYGLAKTWD
     FYQSTFNRSG IRNDGRGAPA YVHVDSSLLN AFYDDDCFCM FFGDGSSQNS NTPVTALDVA
     GHEMSHGVTA ATANLNYSGE SGGLNEATSD IFGTMVEFYA NNSSDPGDYY IGEKLNMPNG
     YMRRMDNPSV DGNSLSCYSS GAGSVDVHYS SGIANHFFYL AAEGTGAKTI GGRSHNGTTC
     NNDTFTGIGR DKAAAVWYRA LTTYMTSTTN YAGARTATLQ AAADLYGANS QERYLVSKAW
     AAVSVGTALP DPGTGSPSPS PSGSTSPSPS PSPSSSGSPN PGNALTNGAF EQGTAGWTQS
     DNDITNSTLQ PAHGGSWYAW MMGYGTSAVE SLSQSNIAVP ASGSPKLTFW LKVSTQESGS
     TAYDTLKVKV NGATLATYSN ANASAGYVQK TVDLSAYKGQ SVKLEFAGTE DAYLATVFLI
     DDVSIG
//
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