ID C0ZYX9_RHOE4 Unreviewed; 517 AA.
AC C0ZYX9;
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:BAH33564.1};
GN OrderedLocusNames=RER_28560 {ECO:0000313|EMBL:BAH33564.1};
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:BAH33564.1, 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:BAH33564.1, 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).
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; AP008957; BAH33564.1; -; Genomic_DNA.
DR RefSeq; WP_020907584.1; NC_012490.1.
DR AlphaFoldDB; C0ZYX9; -.
DR KEGG; rer:RER_28560; -.
DR PATRIC; fig|234621.6.peg.3353; -.
DR eggNOG; COG0596; Bacteria.
DR HOGENOM; CLU_013364_4_0_11; -.
DR Proteomes; UP000002204; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAH33564.1};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..517
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5038616317"
FT DOMAIN 149..297
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT DOMAIN 414..515
FT /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF08386"
FT REGION 29..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 517 AA; 52965 MW; BC5053ACBEA12410 CRC64;
MRRVALMAVV LATCCACGAG PSLRPAVAVE GRTDGSPAQS EGPSPDAPPV DPGVPTDDIP
WRDCTGTSLA DQALAASSAG VILECAEFSA PIDVTGAIDG NFTAGLTRAR TSSTPANAYP
IVFTSGTDRS SGNSLAMLAT SGLTTVLADH PVVALDRRGI DRSTAIDCMT PEIRRGLHDL
GQFDADSTGD AADAVAALGH DATIACTDYL DPQELKFGAD SAAEDIDALR TRWGVETIAL
WSAGSGSDIA LSYAAAHPEN LARLILDSPA PVATDAATEA ESRVQGEEAA LTAFAQRCVA
LGCSLGPDPK KAVTDLMERA RADEFQPLSA AAVSNAISAS LWTAGTNREQ ETRSLSDALS
ALGTGNASPI RERAARAENE VDGDGQFIGR CTDGMQWPGI GRVRELADTW GTNYPVFGRE
AALGLLACAS WPSTANSPLP NQLKPAVLVL SGQGDPAVGN SGLSTVTGVV TNAGSRFATL
DWQGAGHPAA QSTCAQQAMR AYLTDASLPS NGSVCPA
//
