ID C4IPM8_BRUAO Unreviewed; 702 AA.
AC C4IPM8;
DT 07-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 07-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Protease 2 {ECO:0000313|EMBL:EEP64080.1};
GN ORFNames=BAAA_1000610 {ECO:0000313|EMBL:EEP64080.1};
OS Brucella abortus str. 2308 A.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=641140 {ECO:0000313|EMBL:EEP64080.1, ECO:0000313|Proteomes:UP000003313};
RN [1] {ECO:0000313|EMBL:EEP64080.1, ECO:0000313|Proteomes:UP000003313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308 A {ECO:0000313|EMBL:EEP64080.1,
RC ECO:0000313|Proteomes:UP000003313};
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Green L., Rogers Y., Detter J.C., Bruce D., Brettin T.S.;
RL Submitted (MAY-2009) 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:EEP64080.1}.
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DR EMBL; ACOR01000001; EEP64080.1; -; Genomic_DNA.
DR RefSeq; WP_002963718.1; NZ_ACOR01000001.1.
DR AlphaFoldDB; C4IPM8; -.
DR SMR; C4IPM8; -.
DR ESTHER; brume-BMEI1365; S9N_PREPL_Peptidase_S9.
DR MEROPS; S09.010; -.
DR GeneID; 3787319; -.
DR Proteomes; UP000003313; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
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};
KW Protease {ECO:0000313|EMBL:EEP64080.1}.
FT DOMAIN 13..419
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 479..696
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 702 AA; 78274 MW; D444E27C1B10BEA0 CRC64;
MPQDFLRPLP PHAPKHPASD TRHGITRTDD YAWLRAENWQ EVFRDPSVLA PEIRAHLDAE
NAYQAALMKD TENLQKVLFA EMRGRIKEDD SSVPAKDGPY AYGVSYRTGG EQPYFIRTPR
DGGPETILLD GDREGEGKAY FRLASADHAP NHNLLIWGYD DKGSEFYKLK VRDLTTMADL
EDIVTDTNGG GAWDAKSEGF FYTRLDENHR PSKVFYHKIG TQQADDKLIY EETDPGFFLG
VGGSALDDYI FIDIHDHETS ECWLLPADDP SAEPKLVMAR KTGTEYDIAP GGDVFYILTN
ADGAKDFKIC QAPASAPQPE NWQEIVAEKP GRLILSHSAY KHHLVWIERD NGLPRIVIHD
RKTGEEHAIA FDEEAYSLGL HGSAEYDTDV IRFSYSSMTT PEQLFDYNMR TRERTLLKTQ
EVPSGHNPQD YVTRRILAPA FDGELVPVSL LYHKDTKLDG SAPCLLYGYG SYGITIPASF
STSRLSLVDR GFVYAIAHIR GGKDKGFAWY ENGKRDKKTN TFKDFIAAAQ HLVKEGFTSH
DRIVAHGGSA GGMLMGAIAN MAPQAFGGII AEVPFVDVLN TMLDDTLPLT PPEWPEWGNP
IASEADYRTI ASYSPYDNVT AQAYPAILAV AGLTDPRVTY WEPAKWVAKL RELKTDSHPV
LFRINMDAGH AGASGRFSRL EEVAYSFAFA LKVVGKVPSF KN
//
