ID A0A0L0B4X0_9MICC Unreviewed; 731 AA.
AC A0A0L0B4X0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Protease 2 {ECO:0000313|EMBL:KNC15066.1};
DE EC=3.4.21.83 {ECO:0000313|EMBL:KNC15066.1};
GN ORFNames=AC792_15480 {ECO:0000313|EMBL:KNC15066.1};
OS Arthrobacter sp. RIT-PI-e.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1681197 {ECO:0000313|EMBL:KNC15066.1, ECO:0000313|Proteomes:UP000053253};
RN [1] {ECO:0000313|Proteomes:UP000053253}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIT-PI-e {ECO:0000313|Proteomes:UP000053253};
RA Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT "Whole genome sequencing of endophytes isolated from poison ivy
RT (Toxicodendron radicans).";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228}.
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:KNC15066.1}.
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DR EMBL; LGIU01000100; KNC15066.1; -; Genomic_DNA.
DR RefSeq; WP_049831389.1; NZ_LGIU01000100.1.
DR AlphaFoldDB; A0A0L0B4X0; -.
DR STRING; 1681197.AC792_15480; -.
DR PATRIC; fig|1681197.3.peg.737; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000053253; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KNC15066.1};
KW Protease {ECO:0000313|EMBL:KNC15066.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000053253}.
FT DOMAIN 15..442
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 502..718
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 731 AA; 80931 MW; 84DC336D925EB912 CRC64;
MTADAARVPV PVPAPARKVP FERTHHGDTV VDPYEWMREK ESPELLEYLE RENAYTEAVT
QDQASLREAI FTEIKDRTQE TDLSVPARKR GWWYYSRTEE GKQYGIQCRV AAEDTGDLAR
DWTPPEVVPG RPVAGEQVML DGNELAEGKP FFSLGGLSVT EDGTLLAYCE DNAGDERFTL
RIKDLGTGEL LPDEVPNIFY GVAFSPDGTR VYYTVVDDSW RPYQVRSHTL GTPVTDDVVV
YQEDDVAMWT GFEVSADRSE LLISIGCSEY SEYRVLDLAR PEDGLRTLIP RDERILYDAE
PLTIAGVRHY LLTHDRDARN SMVSLVAVDQ LTRPLAEQEW ATVVPHDDAV RVNGASVTST
HVVLSVRKDT IERVQVIPLA GLATSDQQLP AEPDFDEELF PCSLATAEFA SPVIRLSYTS
SPTPPRVHDY VLADGSLELR KETEVRGGYD PADYVAERQW APAADGTLIP LSVIRRAGLA
QDGTNPAVVY AYGSYEASMD PGFSVARLSL LDRGIVYVTA HIRGGGEMGR SWYEQGKKLA
KKNTFTDFVD ATSYLGTSGW VDPARIAAIG GSAGGLLMGA VANLAPEKFR SIVAQVPFVD
ALTTILDPEL PLSALEWEEW GNPITDPEVY RYMKEYTPYE NVRAVDYPRI AAVTSYNDTR
VLYVEPAKWV ARLRETTTGS EPIVLKTEMD GGHGGASGRY SRWRDVAWDY AFTADALGAT
MVLARSTSSV E
//
