ID A0A1A3Q294_9MYCO Unreviewed; 483 AA.
AC A0A1A3Q294;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Peptidase S1 {ECO:0000313|EMBL:OBK40543.1};
GN ORFNames=A5658_21445 {ECO:0000313|EMBL:OBK40543.1};
OS Mycobacterium sp. 1245111.1.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834073 {ECO:0000313|EMBL:OBK40543.1, ECO:0000313|Proteomes:UP000092232};
RN [1] {ECO:0000313|EMBL:OBK40543.1, ECO:0000313|Proteomes:UP000092232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1245111.1 {ECO:0000313|EMBL:OBK40543.1,
RC ECO:0000313|Proteomes:UP000092232};
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 S1C family.
CC {ECO:0000256|ARBA:ARBA00010541}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBK40543.1}.
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; LZLV01000025; OBK40543.1; -; Genomic_DNA.
DR RefSeq; WP_067331890.1; NZ_LZLV01000025.1.
DR AlphaFoldDB; A0A1A3Q294; -.
DR STRING; 1834073.A5658_21445; -.
DR OrthoDB; 9758917at2; -.
DR Proteomes; UP000092232; Unassembled WGS sequence.
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.
DR PROSITE; PS50106; PDZ; 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 86..112
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 387..468
FT /note="PDZ"
FT /evidence="ECO:0000259|PROSITE:PS50106"
FT REGION 1..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 190..236
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..42
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..230
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 48072 MW; D71135824CFDA2CA CRC64;
MTNHPRYSPQ PQQHGYRPGA DQRGAASHSG YGQQQTYGQG YDWRPGQQPP AQQHRQPFGP
FAGQAGHPVG GPPPQHLPMP RKRSRAGALT VGAVAVAVVS AGIGGAAASV VAHHGTLSSV
ADGAMPGGAT PGMPASNAPL GSVEQVAAKV VPSVVMLETN IGRASEEGSG IILSSDGLIL
TNNHVVATAA GKAPGPHARP NPEHQGPDDD PGAPAAPDPD QGPPPPGNGK PKTTVTFSDG
RTAEFTVVGT DPTTDIAVVR VQGMSGLTPI SLGSSANLHV GQPVMAVGSP LGLSGTVTTG
IVSALNRPVS TTGETGNQNT VLDAIQTDAA INPGNSGGAL VNMSGQLVGV NSAIATLGGD
SPDAQSGSIG LGFAIPVDQA KRIADELISS GTASHASLGV QVTNDKETPG AKVVEVVPNG
AAAAAGLPGG VVVTKVDDRT VNSADALVAA VRSKAPGDKV MLTIKDPSGE TKKVQVTLGK
AQQ
//
