ID I2A9G4_9MYCO Unreviewed; 484 AA.
AC I2A9G4;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=PDZ domain-containing protein {ECO:0000259|SMART:SM00228};
GN ORFNames=W7S_04775 {ECO:0000313|EMBL:AFJ33938.1};
OS Mycobacterium sp. MOTT36Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1168287 {ECO:0000313|EMBL:AFJ33938.1, ECO:0000313|Proteomes:UP000002868};
RN [1] {ECO:0000313|EMBL:AFJ33938.1, ECO:0000313|Proteomes:UP000002868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MOTT36Y {ECO:0000313|EMBL:AFJ33938.1,
RC ECO:0000313|Proteomes:UP000002868};
RX PubMed=22815454; DOI=10.1128/JB.00752-12;
RA Kim B.J., Choi B.S., Choi I.Y., Lee J.H., Chun J., Hong S.H., Kook Y.H.,
RA Kim B.J.;
RT "Complete genome sequence of Mycobacterium intracellulare clinical strain
RT MOTT-36Y, belonging to the INT5 genotype.";
RL J. Bacteriol. 194:4141-4142(2012).
CC -!- SIMILARITY: Belongs to the peptidase S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
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DR EMBL; CP003491; AFJ33938.1; -; Genomic_DNA.
DR RefSeq; WP_008254070.1; NC_017904.1.
DR AlphaFoldDB; I2A9G4; -.
DR GeneID; 66743934; -.
DR KEGG; mmm:W7S_04775; -.
DR PATRIC; fig|1168287.3.peg.980; -.
DR HOGENOM; CLU_020120_3_4_11; -.
DR Proteomes; UP000002868; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 2.30.42.10; -; 1.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001940; Peptidase_S1C.
DR PANTHER; PTHR43343; PEPTIDASE S12; 1.
DR PANTHER; PTHR43343:SF3; PROTEASE DO-LIKE 8, CHLOROPLASTIC; 1.
DR Pfam; PF13180; PDZ_2; 1.
DR Pfam; PF13365; Trypsin_2; 1.
DR PRINTS; PR00834; PROTEASES2C.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; PDZ domain-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 103..126
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 396..468
FT /note="PDZ"
FT /evidence="ECO:0000259|SMART:SM00228"
FT REGION 1..96
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..226
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..484
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 22..65
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..226
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 47719 MW; A8071FAC6A703265 CRC64;
MTNDPRYSPP PQQPGYPPAP NQTASVPSHA GSSGYAQGQQ QPYNQQFDWR YRSQPSQTSQ
FRPPYEPFGN TGPGRIPGTG PMPGMLPGMP AAPEPRKRSR AGLLTAGALA IAVVSAGIGG
AAATAIELGD HASGNGGGRV VGAAPSVPAA NMPPGSVEQV ASKVVPSVVM LETDIGRQSE
EGSGIVLSTD GLILTNNHVV AAAAGSPKPP AGLPGAPVPP VAPGGPGGPT PKTTVTFSDG
RTAPFTVVGT DPTSDIAVIR VQGMSGLTPI SLGSSSDLHV GQPVVAIGSP LGLSGTVTTG
IVSALNRPVS TTGESGNQNT VLDAIQTDAA INPGNSGGAL VNMSGQLVGV NSAIATLGGE
SPDAQSGSIG LGFAIPVDQA KRIADELIAT GKASHASLGV QVTSDKGTPG AKVVDVVAGG
AAAAAGVPKN VVVTKVDDRP INSADALVAA VRSKAPGDKI SLTFSDPAGG GSRTLPVTLG
KADQ
//
