ASBC_BACAN
ID ASBC_BACAN Reviewed; 412 AA.
AC Q81RQ7; A0A2P0HD27; E9QYT2; E9QYT3; Q6HZY4; Q6KTW3;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=3,4-dihydroxybenzoate--[aryl-carrier protein] ligase {ECO:0000305};
DE EC=6.2.1.62 {ECO:0000269|PubMed:17346033};
DE AltName: Full=3,4-dihydroxybenzoic acid-AMP ligase {ECO:0000303|PubMed:17346033};
DE AltName: Full=Petrobactin biosynthesis protein AsbC {ECO:0000305};
GN Name=asbC {ECO:0000303|PubMed:17189355};
GN OrderedLocusNames=GBAA_1983 {ECO:0000312|EMBL:AAT31102.1};
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [2]
RP FUNCTION, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=Sterne;
RX PubMed=17189355; DOI=10.1128/jb.01526-06;
RA Lee J.Y., Janes B.K., Passalacqua K.D., Pfleger B.F., Bergman N.H., Liu H.,
RA Haakansson K., Somu R.V., Aldrich C.C., Cendrowski S., Hanna P.C.,
RA Sherman D.H.;
RT "Biosynthetic analysis of the petrobactin siderophore pathway from Bacillus
RT anthracis.";
RL J. Bacteriol. 189:1698-1710(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RC STRAIN=Sterne;
RX PubMed=17346033; DOI=10.1021/bi6023995;
RA Pfleger B.F., Lee J.Y., Somu R.V., Aldrich C.C., Hanna P.C., Sherman D.H.;
RT "Characterization and analysis of early enzymes for petrobactin
RT biosynthesis in Bacillus anthracis.";
RL Biochemistry 46:4147-4157(2007).
RN [4]
RP REVIEW.
RX PubMed=27425635; DOI=10.1111/mmi.13465;
RA Hagan A.K., Carlson P.E. Jr., Hanna P.C.;
RT "Flying under the radar: The non-canonical biochemistry and molecular
RT biology of petrobactin from Bacillus anthracis.";
RL Mol. Microbiol. 102:196-206(2016).
CC -!- FUNCTION: Involved in the biosynthesis of petrobactin, a catecholate
CC siderophore that functions in both iron acquisition and virulence
CC (PubMed:17189355, PubMed:17346033). Catalyzes the adenylation of 3,4-
CC dihydroxybenzoate (3,4-DHBA) to the corresponding AMP ester, followed
CC by the transfer of the activated unit to the phosphopantetheine thiol
CC of the aryl-carrier protein AsbD (PubMed:17346033).
CC {ECO:0000269|PubMed:17189355, ECO:0000269|PubMed:17346033}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoate + ATP + holo-[aryl-carrier protein] =
CC 3,4-dihydroxybenzoyl-[aryl-carrier protein] + AMP + diphosphate;
CC Xref=Rhea:RHEA:62460, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:15941,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:36241,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144963, ChEBI:CHEBI:456215;
CC EC=6.2.1.62; Evidence={ECO:0000269|PubMed:17346033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoate + ATP + H(+) = 3,4-dihydroxybenzoyl-5'-
CC AMP + diphosphate; Xref=Rhea:RHEA:62468, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:36241,
CC ChEBI:CHEBI:144942; Evidence={ECO:0000269|PubMed:17346033};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoyl-5'-AMP + holo-[aryl-carrier protein] =
CC 3,4-dihydroxybenzoyl-[aryl-carrier protein] + AMP + H(+);
CC Xref=Rhea:RHEA:62476, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:15941,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:144942,
CC ChEBI:CHEBI:144963, ChEBI:CHEBI:456215;
CC Evidence={ECO:0000269|PubMed:17346033};
CC -!- ACTIVITY REGULATION: ATP-pyrophosphate exchange is inhibited in vitro
CC by nonhydrolyzable acylsulfamate analogs that mimic the AsbC-bound
CC intermediate 3,4-dihydroxybenzoyl-AMP. {ECO:0000269|PubMed:17346033}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.1 uM for 3,4-DHBA {ECO:0000269|PubMed:17346033};
CC KM=216 uM for ATP {ECO:0000269|PubMed:17346033};
CC Note=kcat is 7.1 min(-1) with 3,4-DHBA as substrate. kcat is 9.1
CC min(-1) with ATP as substrate. {ECO:0000269|PubMed:17346033};
CC -!- PATHWAY: Siderophore biosynthesis; petrobactin biosynthesis.
CC {ECO:0000269|PubMed:17189355, ECO:0000269|PubMed:17346033}.
CC -!- DISRUPTION PHENOTYPE: The deletion mutant cannot produce petrobactin on
CC iron-depleted medium. In vitro analysis show that mutants grow to a
CC very limited extent as vegetative cells in iron-depleted medium but are
CC not able to outgrow from spores under the same culture conditions.
CC {ECO:0000269|PubMed:17189355}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AE017334; AAT31102.1; -; Genomic_DNA.
DR RefSeq; WP_000909602.1; NZ_WXXJ01000029.1.
DR AlphaFoldDB; Q81RQ7; -.
DR SMR; Q81RQ7; -.
DR STRING; 260799.BAS1840; -.
DR DNASU; 1085953; -.
DR EnsemblBacteria; AAT31102; AAT31102; GBAA_1983.
DR GeneID; 45021905; -.
DR KEGG; bar:GBAA_1983; -.
DR PATRIC; fig|1392.230.peg.1943; -.
DR HOGENOM; CLU_670490_0_0_9; -.
DR OMA; EIVVKMN; -.
DR BioCyc; MetaCyc:MON-14943; -.
DR UniPathway; UPA01005; -.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..412
FT /note="3,4-dihydroxybenzoate--[aryl-carrier protein]
FT ligase"
FT /id="PRO_0000450621"
SQ SEQUENCE 412 AA; 46510 MW; DE2AD7189941F423 CRC64;
MLIVNREEYS KSDFDLRLQA YEEMEQFQEA AGNRFALCLK DPFDIITLVF FLKEKKSSVL
LIHEDTPKET AIEMAKRANC IGILYGENSD FTKLEAVNYL AEEPSLLQYS SGTTGEPKLI
RRAWTEVDTE IKVYNEALNC DIDEVPIVMA PVSHSYGLIC GTLSAITRGS KPIIITNKNP
KFALNIVRNT EKHIVYAVPL MLHIMGSFPQ GTFQFHKIMT SGAPLPEALF YKLKETTTYM
MQQYGCSEAG CISICHDMKS HLDLGNPLPH ASISIGSDEN APEEIIVKMN DKEIFTKDLG
YKSERGLHFM GRMDDVINVS GLKVFPIEVE ETMLRLEGVQ EAIVYRGKHP VMGEIVKAKV
ISHIDPVQIR EWCMQHLPSY KVPHEIESVT EIPKNKTGKV SRKLLEMGEV TT
