COATR_MYCTU
ID COATR_MYCTU Reviewed; 394 AA.
AC P96877; F2GKU5; I6Y327; Q7D5S7;
DT 05-JUN-2019, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=Probable fatty acyl-CoA transferase Rv3272 {ECO:0000305};
DE EC=2.8.3.- {ECO:0000305|PubMed:30342240};
GN OrderedLocusNames=Rv3272 {ECO:0000312|EMBL:CCP46091.1};
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3] {ECO:0007744|PDB:5YIT, ECO:0007744|PDB:5YIY, ECO:0007744|PDB:5YX6}
RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF WILD-TYPE AND OF MUTANT ALA-175,
RP FUNCTION, SUBUNIT, DOMAIN, AND ACTIVE SITE.
RC STRAIN=H37Rv;
RX PubMed=30342240; DOI=10.1016/j.bbapap.2018.10.011;
RA Karade S.S., Pandey S., Ansari A., Das S., Tripathi S., Arora A.,
RA Chopra S., Pratap J.V., Dasgupta A.;
RT "Rv3272 encodes a novel family III CoA transferase that alters the cell
RT wall lipid profile and protects mycobacteria from acidic and oxidative
RT stress.";
RL Biochim. Biophys. Acta 1867:317-330(2019).
CC -!- FUNCTION: Probably involved in fatty acid metabolism. Binds to fatty
CC acyl-CoAs of varying carbon chain lengths, with the highest binding
CC affinity for palmitoyl-CoA (C16:0). In vitro, alters the cell wall
CC lipid profile and protects mycobacteria from acidic, oxidative and
CC antibiotic stress. May play a significant role in host-pathogen
CC interaction. {ECO:0000269|PubMed:30342240}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:30342240}.
CC -!- DOMAIN: Consists of a large Rossmann fold domain and a small domain,
CC which are connected by a flexible linker.
CC {ECO:0000269|PubMed:30342240}.
CC -!- SIMILARITY: Belongs to the CoA-transferase III family. {ECO:0000305}.
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DR EMBL; AL123456; CCP46091.1; -; Genomic_DNA.
DR RefSeq; NP_217789.1; NC_000962.3.
DR RefSeq; WP_003417120.1; NZ_NVQJ01000003.1.
DR PDB; 5YIT; X-ray; 2.79 A; A/B/C/D/E=1-394.
DR PDB; 5YIY; X-ray; 2.50 A; A/B=1-394.
DR PDB; 5YX6; X-ray; 2.20 A; A/B/C/D=1-394.
DR PDBsum; 5YIT; -.
DR PDBsum; 5YIY; -.
DR PDBsum; 5YX6; -.
DR AlphaFoldDB; P96877; -.
DR SMR; P96877; -.
DR STRING; 83332.Rv3272; -.
DR PaxDb; P96877; -.
DR PRIDE; P96877; -.
DR DNASU; 888702; -.
DR GeneID; 888702; -.
DR KEGG; mtu:Rv3272; -.
DR PATRIC; fig|83332.111.peg.3654; -.
DR TubercuList; Rv3272; -.
DR eggNOG; COG1804; Bacteria.
DR OMA; NRERHGV; -.
DR PhylomeDB; P96877; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1540.10; -; 1.
DR Gene3D; 3.40.50.10540; -; 1.
DR InterPro; IPR003673; CoA-Trfase_fam_III.
DR InterPro; IPR044855; CoA-Trfase_III_dom3_sf.
DR InterPro; IPR023606; CoA-Trfase_III_dom_1_sf.
DR Pfam; PF02515; CoA_transf_3; 1.
DR SUPFAM; SSF89796; SSF89796; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Transferase.
FT CHAIN 1..394
FT /note="Probable fatty acyl-CoA transferase Rv3272"
FT /id="PRO_0000447345"
FT ACT_SITE 175
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:30342240"
FT TURN 9..12
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 14..17
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 23..33
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 37..42
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 54..56
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 59..62
FT /evidence="ECO:0007829|PDB:5YX6"
FT TURN 64..66
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 67..69
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 83..94
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 107..110
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 115..121
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 126..133
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 135..138
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 146..152
FT /evidence="ECO:0007829|PDB:5YX6"
FT TURN 153..158
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 162..165
FT /evidence="ECO:0007829|PDB:5YIY"
FT HELIX 173..196
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 201..205
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 206..213
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 215..222
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 257..264
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 268..277
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:5YX6"
FT TURN 287..289
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 292..297
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 299..310
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 315..324
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 328..331
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 335..338
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 342..346
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 350..353
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 360..363
FT /evidence="ECO:0007829|PDB:5YX6"
FT STRAND 368..372
FT /evidence="ECO:0007829|PDB:5YX6"
FT TURN 383..386
FT /evidence="ECO:0007829|PDB:5YX6"
FT HELIX 387..390
FT /evidence="ECO:0007829|PDB:5YX6"
SQ SEQUENCE 394 AA; 42459 MW; FF4AE7C448ED5FD3 CRC64;
MPTSNPAKPL DGFRVLDFTQ NVAGPLAGQV LVDLGAEVIK VEAPGGEAAR QITSVLPGRP
PLATYFLPNN RGKKSVTVDL TTEQAKQQML RLADTADVVL EAFRPGTMEK LGLGPDDLRS
RNPNLIYARL TAYGGNGPHG SRPGIDLVVA AEAGMTTGMP TPEGKPQIIP FQLVDNASGH
VLAQAVLAAL LHRERNGVAD VVQVAMYDVA VGLQANQLMM HLNRAASDQP KPEPAPKAKR
RKGVGFATQP SDAFRTADGY IVISAYVPKH WQKLCYLIGR PDLVEDQRFA EQRSRSINYA
ELTAELELAL ASKTATEWVQ LLQANGLMAC LAHTWKQVVD TPLFAENDLT LEVGRGADTI
TVIRTPARYA SFRAVVTDPP PTAGEHNAVF LARP
