ID J9SFK1_9ACTN Unreviewed; 384 AA.
AC J9SFK1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Peptidase M24 {ECO:0000313|EMBL:AFR49019.1};
GN ORFNames=KTR9_2382 {ECO:0000313|EMBL:AFR49019.1};
OS Gordonia sp. KTR9.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=337191 {ECO:0000313|EMBL:AFR49019.1, ECO:0000313|Proteomes:UP000003281};
RN [1] {ECO:0000313|EMBL:AFR49019.1, ECO:0000313|Proteomes:UP000003281}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KTR9 {ECO:0000313|EMBL:AFR49019.1,
RC ECO:0000313|Proteomes:UP000003281};
RX PubMed=22923396; DOI=10.1128/AEM.02120-12;
RA Chen H.P., Zhu S.H., Casabon I., Hallam S.J., Crocker F.H., Mohn W.W.,
RA Indest K.J., Eltis L.D.;
RT "Genomic and transcriptomic studies of an RDX (hexahydro-1,3,5-
RT trinitro-1,3,5-triazine)-degrading actinobacterium.";
RL Appl. Environ. Microbiol. 78:7798-7800(2012).
CC -!- SIMILARITY: Belongs to the peptidase M24B family.
CC {ECO:0000256|RuleBase:RU000590}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002907; AFR49019.1; -; Genomic_DNA.
DR AlphaFoldDB; J9SFK1; -.
DR STRING; 337191.KTR9_2382; -.
DR KEGG; gor:KTR9_2382; -.
DR PATRIC; fig|337191.3.peg.2700; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_1_11; -.
DR Proteomes; UP000003281; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR InterPro; IPR000587; Creatinase_N.
DR InterPro; IPR000994; Pept_M24.
DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU000590}.
FT DOMAIN 22..153
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 161..363
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 384 AA; 40471 MW; B0E71D525DB526E2 CRC64;
MATSEAGAGA APLFGAEVYR DRVRRAAELT RAADLDALVV APGPDLRYLV GSRAETFERL
TALVIPATGD ARLVIARLEV PSLSSSAVGD LDIEVADWVD GDDAHALALA GLPSQPRIAV
SDSMPALHVI PLARHTGATP QLATDVLREL RMIKDAAEID ALRRAGAAID RVHARMGDWL
IPGRTEREVA ADIAAAILEE GHTEAAFIIV GSGPNGADPH HEFSDRVIER SDIVVVDIGG
PVEPGYNSDS TRTYCFDDPP ADIADAYAAL LEAQRAAVAA VRPGVSASSI DAAARDVLAA
RGLAERFIHR TGHGIGLSVH EEPYIVGGND IPLRAGMAFS VEPGVYVSGH WGARIEDIVI
VTDDGCESVN NRPHELVRLD GSNS
//
