ACPM_MYCTU
ID ACPM_MYCTU Reviewed; 115 AA.
AC P9WQF3; L0T917; P0A4W6; Q10500;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 41.
DE RecName: Full=Meromycolate extension acyl carrier protein;
DE Short=ACP;
GN Name=acpM; OrderedLocusNames=Rv2244; ORFNames=MTCY427.25;
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 AS A DRUG TARGET [LARGE SCALE ANALYSIS].
RX PubMed=19099550; DOI=10.1186/1752-0509-2-109;
RA Raman K., Yeturu K., Chandra N.;
RT "targetTB: a target identification pipeline for Mycobacterium tuberculosis
RT through an interactome, reactome and genome-scale structural analysis.";
RL BMC Syst. Biol. 2:109-109(2008).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
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 [4]
RP PHOSPHOPANTETHEINYLATION AT SER-41, AND MUTAGENESIS OF SER-41.
RX PubMed=25785780; DOI=10.1021/bi501444e;
RA Zimhony O., Schwarz A., Raitses-Gurevich M., Peleg Y., Dym O., Albeck S.,
RA Burstein Y., Shakked Z.;
RT "AcpM, the meromycolate extension acyl carrier protein of Mycobacterium
RT tuberculosis, is activated by the 4'-phosphopantetheinyl transferase PptT,
RT a potential target of the multistep mycolic acid biosynthesis.";
RL Biochemistry 54:2360-2371(2015).
CC -!- FUNCTION: Acyl carrier protein involved in meromycolate extension.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- PTM: 4'-phosphopantetheine is transferred from CoA to a specific serine
CC of apo-AcpM by PptT. {ECO:0000269|PubMed:25785780}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC -!- SIMILARITY: Belongs to the acyl carrier protein (ACP) family.
CC {ECO:0000305}.
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DR EMBL; AL123456; CCP45024.1; -; Genomic_DNA.
DR PIR; H70778; H70778.
DR RefSeq; NP_216760.1; NC_000962.3.
DR RefSeq; WP_003411565.1; NZ_NVQJ01000008.1.
DR PDB; 1KLP; NMR; -; A=1-115.
DR PDBsum; 1KLP; -.
DR AlphaFoldDB; P9WQF3; -.
DR SMR; P9WQF3; -.
DR STRING; 83332.Rv2244; -.
DR PaxDb; P9WQF3; -.
DR DNASU; 888272; -.
DR GeneID; 45426224; -.
DR GeneID; 888272; -.
DR KEGG; mtu:Rv2244; -.
DR TubercuList; Rv2244; -.
DR eggNOG; COG0236; Bacteria.
DR OMA; CEIPDEQ; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; HDA:MTBBASE.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0000035; F:acyl binding; IDA:MTBBASE.
DR GO; GO:0000036; F:acyl carrier activity; IDA:MTBBASE.
DR GO; GO:0006637; P:acyl-CoA metabolic process; IDA:MTBBASE.
DR GO; GO:0009245; P:lipid A biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 1.
DR HAMAP; MF_01217; Acyl_carrier; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR003231; Acyl_carrier.
DR InterPro; IPR009081; PP-bd_ACP.
DR PANTHER; PTHR20863; PTHR20863; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SUPFAM; SSF47336; SSF47336; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Phosphopantetheine; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..115
FT /note="Meromycolate extension acyl carrier protein"
FT /id="PRO_0000180247"
FT DOMAIN 3..81
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 41
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258,
FT ECO:0000269|PubMed:25785780"
FT MUTAGEN 41
FT /note="S->A: Abolishes activation by PptT."
FT /evidence="ECO:0000269|PubMed:25785780"
FT HELIX 5..16
FT /evidence="ECO:0007829|PDB:1KLP"
FT TURN 17..20
FT /evidence="ECO:0007829|PDB:1KLP"
FT TURN 24..26
FT /evidence="ECO:0007829|PDB:1KLP"
FT TURN 33..37
FT /evidence="ECO:0007829|PDB:1KLP"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:1KLP"
FT HELIX 61..64
FT /evidence="ECO:0007829|PDB:1KLP"
FT HELIX 70..81
FT /evidence="ECO:0007829|PDB:1KLP"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:1KLP"
SQ SEQUENCE 115 AA; 12524 MW; 2862307DAF6E18D3 CRC64;
MPVTQEEIIA GIAEIIEEVT GIEPSEITPE KSFVDDLDID SLSMVEIAVQ TEDKYGVKIP
DEDLAGLRTV GDVVAYIQKL EEENPEAAQA LRAKIESENP DAVANVQARL EAESK
