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Database: UniProt
Entry: A0A239KLG0_9ACTN
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ID   A0A239KLG0_9ACTN        Unreviewed;       770 AA.
AC   A0A239KLG0;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Zn-dependent metalloprotease {ECO:0000313|EMBL:SNT18905.1};
GN   ORFNames=SAMN05216252_11628 {ECO:0000313|EMBL:SNT18905.1};
OS   Actinacidiphila glaucinigra.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Actinacidiphila.
OX   NCBI_TaxID=235986 {ECO:0000313|EMBL:SNT18905.1, ECO:0000313|Proteomes:UP000198280};
RN   [1] {ECO:0000313|EMBL:SNT18905.1, ECO:0000313|Proteomes:UP000198280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.1858 {ECO:0000313|EMBL:SNT18905.1,
RC   ECO:0000313|Proteomes:UP000198280};
RA   Kim H.J., Triplett B.A.;
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M4 family.
CC       {ECO:0000256|ARBA:ARBA00009388}.
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DR   EMBL; FZOF01000016; SNT18905.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A239KLG0; -.
DR   Proteomes; UP000198280; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProt.
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; 2.60.40.10; Immunoglobulins; 1.
DR   Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR011096; FTP_domain.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR002884; P_dom.
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; PF05345; He_PIG; 1.
DR   Pfam; PF01483; P_proprotein; 1.
DR   Pfam; PF01447; Peptidase_M4; 1.
DR   Pfam; PF02868; Peptidase_M4_C; 1.
DR   PRINTS; PR00730; THERMOLYSIN.
DR   SUPFAM; SSF49313; Cadherin-like; 1.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS51829; P_HOMO_B; 1.
DR   PROSITE; PS51318; TAT; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000313|EMBL:SNT18905.1};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:SNT18905.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198280};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          640..770
FT                   /note="P/Homo B"
FT                   /evidence="ECO:0000259|PROSITE:PS51829"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        369
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        460
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   770 AA;  81585 MW;  A3BC4AF6093E7DF7 CRC64;
     MTSTFRSTRA ASSAARPSGR RRAVATATVT MATLVASVLA LPSAGAQEGP QGTATATASG
     ARSVVLTPVQ RGQLLRAAAG TSAGTAESLK LGDEEKLIPR DVVKDTDGAV HTRYERTFAG
     LPVLGGDLVV HERAGARTVT KASAARLTVP TTEPALAAAK ARTSALDIAG REETRKAAVD
     GAPRLVVWMA TGKPTLAWES VVTGVQKDGT PSRLQVVTDA KTGKQLSSVE QIHAGTGTGQ
     HNGSVRIGTT LNGDVFELVD AERGNSAAYD YDTREVVTDD DDVWGDGTPA DRQTAAVDAA
     YGAQQTWDFF QSRYGRAGIA GDGVGARSYV HVGDGYVNAY WSDACFCMSY GDGENNERPL
     TTLDIAGHEM THGITAATAD LIYSGESGGL NEATSDIMGT AVEFFTNSPK DVPDYLIAEK
     ADVYGTGVPL RYMDQPSKDD VGYGASQDYW SKDTKYLDPH QSSGPANHFF YLLSEGSGKK
     TINGVRYDSP TADGKAVSGI GRESATDIWY RALTVYMTST TDFAGARTAT LQAAADLYGM
     GSAKYETVGN AWAAVNVGYR FVDHIAVDST NPRRTATGQQ VTWQIQAQSS RPGALTYSAK
     GLPRGMSINT RTGLVSGTPV KGGEFRPAIT VKDAAGNCRT VHYQWTVLAS GGDVFVNPNR
     YDIPNWAVIE SPLTVSGRKG NAPADLKVTV DLYAVHVGFY VIDLVSEDGR VIPVKGWSQG
     PVAIPELHQT FTVDASAIPA NGTWKLRVRD NTPGNFIVLP GYLDTWRLGF
//
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