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Database: UniProt
Entry: A0A1C5I559_9ACTN
LinkDB: A0A1C5I559_9ACTN
Original site: A0A1C5I559_9ACTN 
ID   A0A1C5I559_9ACTN        Unreviewed;       801 AA.
AC   A0A1C5I559;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
DE   SubName: Full=Griselysin. Metallo peptidase. MEROPS family M04 {ECO:0000313|EMBL:SCG53327.1};
GN   ORFNames=GA0070613_2266 {ECO:0000313|EMBL:SCG53327.1};
OS   Micromonospora inositola.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=47865 {ECO:0000313|EMBL:SCG53327.1, ECO:0000313|Proteomes:UP000198221};
RN   [1] {ECO:0000313|EMBL:SCG53327.1, ECO:0000313|Proteomes:UP000198221}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43819 {ECO:0000313|EMBL:SCG53327.1,
RC   ECO:0000313|Proteomes:UP000198221};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; LT607754; SCG53327.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5I559; -.
DR   OrthoDB; 345880at2; -.
DR   Proteomes; UP000198221; Chromosome i.
DR   GO; GO:0004222; F:metalloendopeptidase 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; IPR011096; FTP_domain.
DR   InterPro; IPR013783; Ig-like_fold.
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};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW   Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000198221};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           28..801
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008718356"
FT   DOMAIN          61..102
FT                   /note="FTP"
FT                   /evidence="ECO:0000259|Pfam:PF07504"
FT   DOMAIN          200..343
FT                   /note="Peptidase M4"
FT                   /evidence="ECO:0000259|Pfam:PF01447"
FT   DOMAIN          349..526
FT                   /note="Peptidase M4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02868"
FT   ACT_SITE        336
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
FT   ACT_SITE        425
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR623612-1"
SQ   SEQUENCE   801 AA;  81694 MW;  EAE0775485393BE1 CRC64;
     MKRPLAAFGA ALLTSGVLTC VATAAHAATP SGPAPESSAA ARADNLLRSN PGAVQGASGE
     AYQAVRTKVD ASGAAHTRYT RTYHGLRVYG GDFVIHTAPD GSYAGTSVGL AAPLTLGTSA
     KVGGPAAKAS ARGAFSGSLT SVGAPELFVD ASSGRGRLAW ETVASGWKAD KQTPSKLHVI
     TDATTGKVIG SYDEIETVAG TGNSLYSGTV SIDTTLSGST YQMIDPSHGN GRTCDMNNGT
     FTCTTFTDAD NTWGTGANSN RQSAAVDAHF GAAKTFDYYK NVHARNGIFG NGTGVPSRVH
     YGNNYVNAFW DGSQMTYGDG SGNARPLVAL DVAGHEMSHG VTENVVPGGL TYSGESGGLN
     EATSDIFGTM VEFYANTTAD PGDYQIGEKI NINGNGTPLR YMYNPALDGS SDSCWSTSTK
     NKDVHYSSGP ANHFFFNLAE GTGATAYGTS PVCGSAPAVT GIGRARAEKI WFRALDVYFT
     SNTSYVNNTT PSNTARAYSL RAATDLYGNC STEYKTVQAA WTAVNVAGND APCSSTGNDF
     SVALSPTSGS VTAGGSVSTT VSTATTSGTA QTVTFSASGL PSGASASFSP SSVTSGGSST
     LTISTTSGTA AGTYSVTVTG TATSGSHSAT YTLTVNGTGG GCTGAGQKLG NPGFESGNTV
     WASTSGVIGQ YGSSGQPTHG GTWNAWLDGY GTSHTDTLSQ SVSLPAGCTS YNFSFWLHID
     TSETTTGTAY DTLRVQVLNS SGTVLATLAT YSNLNRAAGY SQKSFSLASY AGQTVTLKFT
     GVEDISLQTS FVVDDTAVNV S
//
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