ID C0ZT68_RHOE4 Unreviewed; 646 AA.
AC C0ZT68;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Putative hydrolase {ECO:0000313|EMBL:BAH32041.1};
GN OrderedLocusNames=RER_13330 {ECO:0000313|EMBL:BAH32041.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH32041.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH32041.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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DR EMBL; AP008957; BAH32041.1; -; Genomic_DNA.
DR RefSeq; WP_020906585.1; NC_012490.1.
DR AlphaFoldDB; C0ZT68; -.
DR MEROPS; S09.072; -.
DR KEGG; rer:RER_13330; -.
DR PATRIC; fig|234621.6.peg.1805; -.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_012236_1_0_11; -.
DR Proteomes; UP000002204; Chromosome.
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; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR43056:SF5; ACYL-PEPTIDE HYDROLASE; 1.
DR PANTHER; PTHR43056; PEPTIDASE S9 PROLYL OLIGOPEPTIDASE; 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, ECO:0000313|EMBL:BAH32041.1}.
FT DOMAIN 424..628
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 646 AA; 69319 MW; F955B30DD4F551F9 CRC64;
MTPSEQIAAP YGSWTSPIGA ADLAAGGHPV EGGRYVGDEI WWAELRPTEG GRTSIRRSGL
DNQPVDILPA PWNARTRVHE YGGGAWTVTE SGKLVFSEFS DQRVYILEGV TPRALTPEPA
SPAALRYADL QIVNGEVWAV REAHAEGGAI TRDICAIPLD GSGKVRSIVG GSDFLSSPRL
SPSGTKIAWI AWNHPQMPWD GTELRVAPLV DGVAQNYSVL IGGLEESVLQ PEWITDDELY
AISDRSGWWN IYRVGGKITP ICPVNADFGG PQWRFGARWF VELDNGHLLT ARTVGTDTLA
VLDPASGELR DIAIPGVTSI GLMQVRGDRL LLTSGGAKLA GALREFDLGT GELTEIRSSV
EELPESAYLP EARAVVAHGH GREVHAVAYP PRSPRYKGLD GELPPYVAFV HGGPTAHVAP
ALNLVYAFFT SRGIGVVDVN YGGSTGYGRE YRNRLRGQWG VVDVQDVVTA VTGLAEQGLA
DPARLAIEGG SAGGWTVLAA LTTSDVFACG ASYFGVAELD LFVQETHDFE SRYVDGLIGP
LPESADLYAE RAPLNNVDGL NCPVLLLQGL DDPIVPPSQA ERFRDALVTK GIPHAYLAYE
GESHGFRKQS TIISSRNAEL SFYGQVLGFI PPGIPTLELW KPAISS
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