ID A0A0H2KRI3_9MICO Unreviewed; 770 AA.
AC A0A0H2KRI3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Peptidase S9 {ECO:0000313|EMBL:KLN35783.1};
GN ORFNames=FB00_05705 {ECO:0000313|EMBL:KLN35783.1};
OS Cellulosimicrobium funkei.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC Promicromonosporaceae; Cellulosimicrobium.
OX NCBI_TaxID=264251 {ECO:0000313|EMBL:KLN35783.1, ECO:0000313|Proteomes:UP000035265};
RN [1] {ECO:0000313|EMBL:KLN35783.1, ECO:0000313|Proteomes:UP000035265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=U11 {ECO:0000313|EMBL:KLN35783.1,
RC ECO:0000313|Proteomes:UP000035265};
RA Hu C., Gong Y., Wan W., Jiang M.;
RT "Cellulosimicrobium funkei U11 genome.";
RL Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
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:KLN35783.1}.
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DR EMBL; JNBQ01000003; KLN35783.1; -; Genomic_DNA.
DR RefSeq; WP_047231856.1; NZ_JNBQ01000003.1.
DR AlphaFoldDB; A0A0H2KRI3; -.
DR STRING; 264251.FB00_05705; -.
DR PATRIC; fig|264251.5.peg.1169; -.
DR Proteomes; UP000035265; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 2.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000035265}.
FT DOMAIN 544..753
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 74..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 81825 MW; A69873B3250E3A27 CRC64;
MSNDAATPGT SDQPESPFHD LDQYLAIPRV GGLALSPDGA RLVTTVQTLD PQRTGYRTAL
WEVDPAGEVP ARRLTRSTKG ESSATFTGAG DVLFTSARPD PDGGSDDDPK AALWLLPATG
GEARVVATAP AGVSGPLAAA DAPVVSVAAS VLPSARDLAH DAELRSARKD AKVAAILHSA
YPVRQWDHDR GPDEAHRFVG DLTTLVDEPA HPLPDPAGTS GAEPGGTDVT DDHGPHDPRL
LDLRDVTRGV EQGTAPGRAL HEHSADLSGD GTTLVTTWQV AGPGPQVRNT LVAIDTATGA
RRTLVDEPSA EAHSPRISPD GAWVAFVRET ISTPHQAPEE SLAVVPLHAP DGPAGAVEGH
DDSATTRAEN HATPRTLVPH WDRWPTSLRW LPDGSGLLVT ADDDGRGPVF LVAFSPDGTT
ENGTAERVTS DDAVFTDVQV APDGRTAYAL RTSYLEPSHP VRIDLGAFLG SGAAGGRTPV
PATPLRGPVA TPDLPGTLVD VETAASDDVR VRGWLALPHG ASADDPAPLL LWIHGGPLGS
WNAWSWRWNP WLMVARGYAV LLPDPALSTG YGQDFVQRGW GSWGKAPYTD LLAITDAVEA
RPEVDATRTA AMGGSFGGYM ANWVAGHTDR FRAVVTHASL WALDQFGPTT DHAYYWAREM
TPEMAFENSP HRFVGDIVTP MLVIHGDKDY RVPIGEGLRL WYELLESSGL PAGADSETVH
RFLFYPDENH WILQPQHAKV WYQVVLAFLA EHVLGATPGE GDAALPTTLG
//
