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
//