Y2247_MYCBO
ID Y2247_MYCBO Reviewed; 520 AA.
AC P65822; A0A1R3Y1B5; Q10508; X2BKG1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 25-MAY-2022, entry version 94.
DE RecName: Full=Putative hydrolase Mb2247c;
DE EC=3.4.-.-;
DE Flags: Precursor;
GN OrderedLocusNames=BQ2027_MB2247C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR EMBL; LT708304; SIU00855.1; -; Genomic_DNA.
DR RefSeq; NP_855896.1; NC_002945.3.
DR RefSeq; WP_003411484.1; NC_002945.4.
DR AlphaFoldDB; P65822; -.
DR SMR; P65822; -.
DR ESTHER; myctu-ym23; AlphaBeta_hydrolase.
DR EnsemblBacteria; SIU00855; SIU00855; BQ2027_MB2247C.
DR PATRIC; fig|233413.5.peg.2464; -.
DR OMA; NQMAGFQ; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR013595; Pept_S33_TAP-like_C.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR Pfam; PF08386; Abhydrolase_4; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 3: Inferred from homology;
KW Cell membrane; Hydrolase; Membrane; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..34
FT /evidence="ECO:0000255"
FT CHAIN 35..520
FT /note="Putative hydrolase Mb2247c"
FT /id="PRO_0000027328"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 105..403
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 232
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 461
FT /evidence="ECO:0000250"
FT ACT_SITE 488
FT /note="Proton donor"
FT /evidence="ECO:0000250"
SQ SEQUENCE 520 AA; 55078 MW; 7D05F1533A4C6B91 CRC64;
MAAMWRRRPL SSALLSFGLL LGGLPLAAPP LAGATEEPGA GQTPGAPVVA PQQSWNSCRE
FIADTSEIRT ARCATVSVPV DYDQPGGTQA KLAVIRVPAT GQRFGALLVN PGGPGASAVD
MVAAMAPAIA DTDILRHFDL VGFDPRGVGH STPALRCRTD AEFDAYRRDP MADYSPAGVT
HVEQVYRQLA QDCVDRMGFS FLANIGTASV ARDMDMVRQA LGDDQINYLG YSYGTELGTA
YLERFGTHVR AMVLDGAIDP AVSPIEESIS QMAGFQTAFN DYAADCARSP ACPLGTDSAQ
WVNRYHALVD PLVQKPGKTS DPRGLSYADA TTGTINALYS PQRWKYLTSG LLGLQRGSDA
GDLLVLADDY DGRDADGHYS NDQDAFNAVR CVDAPTPADP AAWVAADQRI RQVAPFLSYG
QFTGSAPRDL CALWPVPATS TPHPAAPAGA GKVVVVSTTH DPATPYQSGV DLARQLGAPL
ITFDGTQHTA VFDGNQCVDS AVMHYFLDGT LPPTSLRCAP