ASBE_BACAN
ID ASBE_BACAN Reviewed; 327 AA.
AC Q81RQ5; E9R8M9; Q6KTW1;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Petrobactin synthase {ECO:0000305};
DE EC=2.3.2.- {ECO:0000269|PubMed:22408253};
DE AltName: Full=Petrobactin biosynthesis protein AsbE {ECO:0000305};
GN Name=asbE {ECO:0000303|PubMed:17189355};
GN OrderedLocusNames=GBAA_1985 {ECO:0000312|EMBL:AAT31104.1};
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, 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 FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RC STRAIN=Sterne;
RX PubMed=22408253; DOI=10.1074/jbc.m112.359349;
RA Nusca T.D., Kim Y., Maltseva N., Lee J.Y., Eschenfeldt W., Stols L.,
RA Schofield M.M., Scaglione J.B., Dixon S.D., Oves-Costales D., Challis G.L.,
RA Hanna P.C., Pfleger B.F., Joachimiak A., Sherman D.H.;
RT "Functional and structural analysis of the siderophore synthetase AsbB
RT through reconstitution of the petrobactin biosynthetic pathway from
RT Bacillus anthracis.";
RL J. Biol. Chem. 287:16058-16072(2012).
RN [5]
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, PubMed:22408253). Transfers the
CC activated 3,4-dihydroxybenzoate (3,4-DHBA) moiety from 3,4-DHBA-loaded
CC AsbD to different receipient molecules, including N-citryl-spermidine,
CC N8,N'8-citryl-bis(spermidine) and N1-(3,4-dihydroxybenzoyl)-N8,N'8-
CC citryl-bis(spermidine) (PubMed:22408253). Also catalyzes the transfer
CC of the activated 3,4-DHBA moiety from 3,4-DHBA-loaded AsbD to
CC spermidine to generate DHB-spermidine (DHB-SP) (PubMed:17346033).
CC {ECO:0000269|PubMed:17189355, ECO:0000269|PubMed:17346033,
CC ECO:0000269|PubMed:22408253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoyl-[aryl-carrier protein] + N(8)-citryl-
CC spermidine = H(+) + holo-[aryl-carrier protein] + N(1)-(3,4-
CC dihydroxybenzoyl)-N(8)-citryl-spermidine; Xref=Rhea:RHEA:64028,
CC Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:15941, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144963, ChEBI:CHEBI:149586,
CC ChEBI:CHEBI:149593; Evidence={ECO:0000269|PubMed:22408253};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoyl-[aryl-carrier protein] + N(8),N'(8)-
CC citryl-bis(spermidine) = H(+) + holo-[aryl-carrier protein] + N(1)-
CC (3,4-dihydroxybenzoyl)-N(8),N'(8)-citryl-bis(spermidine);
CC Xref=Rhea:RHEA:64024, Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:15941,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:64479, ChEBI:CHEBI:144963,
CC ChEBI:CHEBI:149592, ChEBI:CHEBI:149594;
CC Evidence={ECO:0000269|PubMed:22408253};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3,4-dihydroxybenzoyl-[aryl-carrier protein] + N(1)-(3,4-
CC dihydroxybenzoyl)-N(8),N'(8)-citryl-bis(spermidine) = H(+) + holo-
CC [aryl-carrier protein] + petrobactin; Xref=Rhea:RHEA:63820,
CC Rhea:RHEA-COMP:15903, Rhea:RHEA-COMP:15941, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:142778, ChEBI:CHEBI:144963,
CC ChEBI:CHEBI:149594; Evidence={ECO:0000269|PubMed:22408253};
CC -!- PATHWAY: Siderophore biosynthesis; petrobactin biosynthesis.
CC {ECO:0000269|PubMed:17189355, ECO:0000269|PubMed:17346033,
CC ECO:0000269|PubMed:22408253}.
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}.
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DR EMBL; AE017334; AAT31104.1; -; Genomic_DNA.
DR RefSeq; WP_000200715.1; NZ_WXXJ01000029.1.
DR AlphaFoldDB; Q81RQ5; -.
DR STRING; 260799.BAS1842; -.
DR DNASU; 1085949; -.
DR EnsemblBacteria; AAT31104; AAT31104; GBAA_1985.
DR GeneID; 45021907; -.
DR KEGG; bar:GBAA_1985; -.
DR PATRIC; fig|1392.230.peg.1945; -.
DR HOGENOM; CLU_052637_0_0_9; -.
DR OMA; QNPFPHY; -.
DR BioCyc; MetaCyc:MON-14944; -.
DR UniPathway; UPA01005; -.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0016746; F:acyltransferase activity; IEA:UniProtKB-KW.
DR InterPro; IPR046047; DUF6005.
DR Pfam; PF19468; DUF6005; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Reference proteome; Transferase.
FT CHAIN 1..327
FT /note="Petrobactin synthase"
FT /id="PRO_0000450625"
SQ SEQUENCE 327 AA; 39032 MW; 5536B01879CD8296 CRC64;
MTSIKVHCLV SCFCEIIKRR SDIDFRPFYF GLWDGDFDIT EGGIISYHSE NINHDHYLLW
YEKLYGMKVN EWYDHAKDKD SNVETFLQLV ENKPENRYVI VMVDMSLLPE RENKFHQKPF
PHYLMISETE KEEEWFMLDP DFRWEGNMER EKVLYSVQDN PFGGGYFIDV EEIQEPTAEM
VASYFIETFK RNDNELTMEL KNLIIKMANE EEGYLLSGLV AAVKQIPVLA IRKYSYEHAF
AYFRETLQYS EQEFDYWCDR VEDIVQGFTN VQYRAIKMAM TNNKGMLLSI VEKLDEMNAI
ELQIKTELER QFLSWKEMKS NESVLVF
