ACPS_MYCTU
ID ACPS_MYCTU Reviewed; 130 AA.
AC P9WQD3; L0TCS3; O53228; P0A4W8;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 49.
DE RecName: Full=Holo-[acyl-carrier-protein] synthase {ECO:0000255|HAMAP-Rule:MF_00101};
DE Short=Holo-ACP synthase {ECO:0000255|HAMAP-Rule:MF_00101};
DE EC=2.7.8.7 {ECO:0000255|HAMAP-Rule:MF_00101, ECO:0000269|PubMed:21697604, ECO:0000305|PubMed:16709676};
DE AltName: Full=4'-phosphopantetheinyl transferase AcpS {ECO:0000255|HAMAP-Rule:MF_00101};
GN Name=acpS {ECO:0000255|HAMAP-Rule:MF_00101}; OrderedLocusNames=Rv2523c;
GN ORFNames=MTV009.08c;
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 SUBUNIT, AND CRYSTALLIZATION.
RC STRAIN=H37Rv;
RX PubMed=11752806; DOI=10.1107/s0907444901019874;
RA Chopra S., Singh S.K., Sati S.P., Ranganathan A., Sharma A.;
RT "Expression, purification, crystallization and preliminary X-ray analysis
RT of the acyl carrier protein synthase (acpS) from Mycobacterium
RT tuberculosis.";
RL Acta Crystallogr. D 58:179-181(2002).
RN [3]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=16709676; DOI=10.1073/pnas.0511129103;
RA Chalut C., Botella L., de Sousa-D'Auria C., Houssin C., Guilhot C.;
RT "The nonredundant roles of two 4'-phosphopantetheinyl transferases in vital
RT processes of Mycobacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:8511-8516(2006).
RN [4]
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 [5]
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 [6] {ECO:0007744|PDB:3HQJ}
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH COENZYME A AND
RP MAGNESIUM, COFACTOR, AND SUBUNIT.
RX PubMed=19733180; DOI=10.1016/j.jmb.2009.08.065;
RA Dym O., Albeck S., Peleg Y., Schwarz A., Shakked Z., Burstein Y.,
RA Zimhony O.;
RT "Structure-function analysis of the acyl carrier protein synthase (AcpS)
RT from Mycobacterium tuberculosis.";
RL J. Mol. Biol. 393:937-950(2009).
RN [7] {ECO:0007744|PDB:3H7Q}
RP X-RAY CRYSTALLOGRAPHY (2.25 ANGSTROMS).
RA Poulsen C., Wilmanns M., Song Y.H.;
RT "Structure of the holo-[Acyl-Carrier-Protein] Synthase (ACPS) from
RT Mycobacterium.";
RL Submitted (APR-2009) to the PDB data bank.
RN [8] {ECO:0007744|PDB:3NE1, ECO:0007744|PDB:3NE3}
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
RC STRAIN=H37Rv;
RX PubMed=21697604; DOI=10.1107/s0907444911020221;
RA Gokulan K., Aggarwal A., Shipman L., Besra G.S., Sacchettini J.C.;
RT "Mycobacterium tuberculosis acyl carrier protein synthase adopts two
RT different pH-dependent structural conformations.";
RL Acta Crystallogr. D 67:657-669(2011).
RN [9] {ECO:0007744|PDB:4HC6}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 2-130 OF MUTANT ALA-77.
RA Kim H.-B., Han G.-W., Hung L.-W., Terwilliger C.T., Kim C.-Y.;
RT "Mycobacterium tuberculosis Rv2523c E77A x-ray structure solved with 1.8
RT angstrom resolution.";
RL Submitted (SEP-2012) to the PDB data bank.
CC -!- FUNCTION: Transfers the 4'-phosphopantetheine moiety from coenzyme A to
CC a Ser of acyl-carrier-protein (PubMed:16709676, PubMed:21697604).
CC Involved in the post-translational modification of Fas-I and the AcpM
CC subunit of Fas-II (PubMed:21697604). {ECO:0000269|PubMed:16709676,
CC ECO:0000269|PubMed:21697604}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=apo-[ACP] + CoA = adenosine 3',5'-bisphosphate + H(+) + holo-
CC [ACP]; Xref=Rhea:RHEA:12068, Rhea:RHEA-COMP:9685, Rhea:RHEA-
CC COMP:9690, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:57287,
CC ChEBI:CHEBI:58343, ChEBI:CHEBI:64479; EC=2.7.8.7;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00101,
CC ECO:0000269|PubMed:21697604, ECO:0000305|PubMed:16709676};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00101,
CC ECO:0000269|PubMed:19733180};
CC Note=Binds 2 Mg(2+) per subunit. {ECO:0000269|PubMed:19733180};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is between 4.4 and 6.0. {ECO:0000269|PubMed:21697604};
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:11752806,
CC ECO:0000269|PubMed:19733180}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00101}.
CC -!- DOMAIN: Apo-AcpS adopts different conformations depending upon the pH
CC conditions of the crystallization solution.
CC {ECO:0000269|PubMed:21697604}.
CC -!- MISCELLANEOUS: Was identified as a high-confidence drug target.
CC {ECO:0000269|PubMed:19099550}.
CC -!- SIMILARITY: Belongs to the P-Pant transferase superfamily. AcpS family.
CC {ECO:0000255|HAMAP-Rule:MF_00101}.
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DR EMBL; AL123456; CCP45317.1; -; Genomic_DNA.
DR PIR; H70870; H70870.
DR RefSeq; NP_217039.1; NC_000962.3.
DR RefSeq; WP_003412952.1; NZ_NVQJ01000032.1.
DR PDB; 3H7Q; X-ray; 2.25 A; A=1-130.
DR PDB; 3HQJ; X-ray; 1.95 A; A=1-130.
DR PDB; 3NE1; X-ray; 2.51 A; A/B/C=1-130.
DR PDB; 3NE3; X-ray; 1.90 A; B=1-130.
DR PDB; 4HC6; X-ray; 1.80 A; A=2-130.
DR PDBsum; 3H7Q; -.
DR PDBsum; 3HQJ; -.
DR PDBsum; 3NE1; -.
DR PDBsum; 3NE3; -.
DR PDBsum; 4HC6; -.
DR AlphaFoldDB; P9WQD3; -.
DR SMR; P9WQD3; -.
DR STRING; 83332.Rv2523c; -.
DR PaxDb; P9WQD3; -.
DR DNASU; 888626; -.
DR GeneID; 45426523; -.
DR GeneID; 888626; -.
DR KEGG; mtu:Rv2523c; -.
DR TubercuList; Rv2523c; -.
DR eggNOG; COG0736; Bacteria.
DR OMA; NTCGLGH; -.
DR BRENDA; 2.7.8.7; 3445.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008897; F:holo-[acyl-carrier-protein] synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.90.470.20; -; 1.
DR HAMAP; MF_00101; AcpS; 1.
DR InterPro; IPR008278; 4-PPantetheinyl_Trfase_dom.
DR InterPro; IPR037143; 4-PPantetheinyl_Trfase_dom_sf.
DR InterPro; IPR002582; ACPS.
DR InterPro; IPR004568; Ppantetheine-prot_Trfase_dom.
DR Pfam; PF01648; ACPS; 1.
DR SUPFAM; SSF56214; SSF56214; 1.
DR TIGRFAMs; TIGR00556; pantethn_trn; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Fatty acid biosynthesis; Fatty acid metabolism;
KW Lipid biosynthesis; Lipid metabolism; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..130
FT /note="Holo-[acyl-carrier-protein] synthase"
FT /id="PRO_0000175675"
FT BINDING 9
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:19733180"
FT BINDING 53
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:19733180,
FT ECO:0007744|PDB:3HQJ"
FT BINDING 115..116
FT /ligand="CoA"
FT /ligand_id="ChEBI:CHEBI:57287"
FT /evidence="ECO:0000269|PubMed:19733180,
FT ECO:0007744|PDB:3HQJ"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:19733180,
FT ECO:0007744|PDB:3HQJ"
FT STRAND 3..12
FT /evidence="ECO:0007829|PDB:4HC6"
FT HELIX 13..20
FT /evidence="ECO:0007829|PDB:4HC6"
FT STRAND 22..25
FT /evidence="ECO:0007829|PDB:4HC6"
FT HELIX 26..29
FT /evidence="ECO:0007829|PDB:4HC6"
FT HELIX 33..39
FT /evidence="ECO:0007829|PDB:4HC6"
FT HELIX 45..66
FT /evidence="ECO:0007829|PDB:4HC6"
FT TURN 67..70
FT /evidence="ECO:0007829|PDB:4HC6"
FT TURN 76..78
FT /evidence="ECO:0007829|PDB:3NE3"
FT HELIX 79..82
FT /evidence="ECO:0007829|PDB:4HC6"
FT STRAND 83..87
FT /evidence="ECO:0007829|PDB:4HC6"
FT STRAND 93..97
FT /evidence="ECO:0007829|PDB:4HC6"
FT HELIX 100..104
FT /evidence="ECO:0007829|PDB:4HC6"
FT TURN 105..107
FT /evidence="ECO:0007829|PDB:4HC6"
FT STRAND 109..117
FT /evidence="ECO:0007829|PDB:4HC6"
FT STRAND 120..128
FT /evidence="ECO:0007829|PDB:4HC6"
SQ SEQUENCE 130 AA; 14003 MW; 7DDA3A856F1F9618 CRC64;
MGIVGVGIDL VSIPDFAEQV DQPGTVFAET FTPGERRDAS DKSSSAARHL AARWAAKEAV
IKAWSGSRFA QRPVLPEDIH RDIEVVTDMW GRPRVRLTGA IAEYLADVTI HVSLTHEGDT
AAAVAILEAP
