ASBB_BACAN
ID ASBB_BACAN Reviewed; 612 AA.
AC Q81RQ8; E9QRE2; Q6KTW4;
DT 12-AUG-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Citryl-spermidine/3,4-dihydroxybenzoyl-citryl-spermidine:spermidine ligase {ECO:0000305};
DE EC=6.3.2.- {ECO:0000269|PubMed:18758617, ECO:0000269|PubMed:22408253};
DE AltName: Full=Petrobactin biosynthesis protein AsbB {ECO:0000305};
GN Name=asbB {ECO:0000303|PubMed:14756782};
GN OrderedLocusNames=GBAA_1982 {ECO:0000312|EMBL:AAT31101.2};
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 GENE NAME.
RC STRAIN=Sterne;
RX PubMed=14756782; DOI=10.1046/j.1365-2958.2003.03861.x;
RA Cendrowski S., MacArthur W., Hanna P.;
RT "Bacillus anthracis requires siderophore biosynthesis for growth in
RT macrophages and mouse virulence.";
RL Mol. Microbiol. 51:407-417(2004).
RN [3]
RP FUNCTION.
RC STRAIN=Sterne;
RX PubMed=16875672; DOI=10.1016/j.bbrc.2006.07.055;
RA Wilson M.K., Abergel R.J., Raymond K.N., Arceneaux J.E., Byers B.R.;
RT "Siderophores of Bacillus anthracis, Bacillus cereus, and Bacillus
RT thuringiensis.";
RL Biochem. Biophys. Res. Commun. 348:320-325(2006).
RN [4]
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 [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=18758617; DOI=10.1039/b809353a;
RA Oves-Costales D., Kadi N., Fogg M.J., Song L., Wilson K.S., Challis G.L.;
RT "Petrobactin biosynthesis: AsbB catalyzes condensation of spermidine with
RT N8-citryl-spermidine and its N1-(3,4-dihydroxybenzoyl) derivative.";
RL Chem. Commun. (Camb.) 34:4034-4036(2008).
RN [6]
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).
RN [7] {ECO:0007744|PDB:3TO3}
RP X-RAY CRYSTALLOGRAPHY (2.38 ANGSTROMS) OF 3-612 IN COMPLEX WITH ATP,
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, PATHWAY, AND MUTAGENESIS OF LYS-313
RP AND GLU-461.
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).
CC -!- FUNCTION: Involved in the biosynthesis of petrobactin, a catecholate
CC siderophore that functions in both iron acquisition and virulence
CC (PubMed:16875672, PubMed:17189355, PubMed:22408253). Catalyzes the ATP-
CC dependent condensation of spermidine with N(8)-citryl-spermidine or
CC N(1)-(3,4-dihydroxbenzoyl)-N(8)-citryl-spermidine, two intermediates in
CC petrobactin biosynthesis pathway (PubMed:18758617, PubMed:22408253).
CC {ECO:0000269|PubMed:16875672, ECO:0000269|PubMed:17189355,
CC ECO:0000269|PubMed:18758617, ECO:0000269|PubMed:22408253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(8)-citryl-spermidine + spermidine = AMP + diphosphate
CC + H(+) + N(8),N'(8)-citryl-bis(spermidine); Xref=Rhea:RHEA:63812,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:149586, ChEBI:CHEBI:149592,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18758617,
CC ECO:0000269|PubMed:22408253};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N(1)-(3,4-dihydroxybenzoyl)-N(8)-citryl-spermidine +
CC spermidine = AMP + diphosphate + H(+) + N(1)-(3,4-dihydroxybenzoyl)-
CC N(8),N'(8)-citryl-bis(spermidine); Xref=Rhea:RHEA:63816,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57834, ChEBI:CHEBI:149593, ChEBI:CHEBI:149594,
CC ChEBI:CHEBI:456215; Evidence={ECO:0000269|PubMed:18758617,
CC ECO:0000269|PubMed:22408253};
CC -!- PATHWAY: Siderophore biosynthesis; petrobactin biosynthesis.
CC {ECO:0000269|PubMed:17189355, ECO:0000269|PubMed:18758617,
CC ECO:0000269|PubMed:22408253}.
CC -!- SUBUNIT: Homodimer. {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}.
CC -!- SIMILARITY: Belongs to the IucA/IucC family. {ECO:0000305}.
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DR EMBL; AE017334; AAT31101.2; -; Genomic_DNA.
DR RefSeq; WP_011053144.1; NZ_WXXJ01000029.1.
DR PDB; 3TO3; X-ray; 2.38 A; A/B=3-612.
DR PDBsum; 3TO3; -.
DR AlphaFoldDB; Q81RQ8; -.
DR SMR; Q81RQ8; -.
DR STRING; 260799.BAS1839; -.
DR DNASU; 1083942; -.
DR EnsemblBacteria; AAT31101; AAT31101; GBAA_1982.
DR GeneID; 45021904; -.
DR KEGG; bar:GBAA_1982; -.
DR PATRIC; fig|1392.230.peg.1942; -.
DR HOGENOM; CLU_018524_0_1_9; -.
DR BioCyc; MetaCyc:MON-14941; -.
DR UniPathway; UPA01005; -.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0016881; F:acid-amino acid ligase activity; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019290; P:siderophore biosynthetic process; IEA:InterPro.
DR InterPro; IPR007310; Aerobactin_biosyn_IucA/IucC_N.
DR InterPro; IPR022770; FhuF_domain.
DR InterPro; IPR037455; LucA/IucC-like.
DR PANTHER; PTHR34384; PTHR34384; 1.
DR Pfam; PF06276; FhuF; 1.
DR Pfam; PF04183; IucA_IucC; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..612
FT /note="Citryl-spermidine/3,4-dihydroxybenzoyl-citryl-
FT spermidine:spermidine ligase"
FT /id="PRO_0000450624"
FT BINDING 282..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22408253,
FT ECO:0007744|PDB:3TO3"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22408253,
FT ECO:0007744|PDB:3TO3"
FT BINDING 310
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22408253,
FT ECO:0007744|PDB:3TO3"
FT BINDING 390
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22408253,
FT ECO:0007744|PDB:3TO3"
FT BINDING 461
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:22408253,
FT ECO:0007744|PDB:3TO3"
FT MUTAGEN 313
FT /note="K->A: Preference for spermidine is not completely
FT abrogated, but activity is increased with unnatural
FT nucleophiles such as spermine, l,8-diaminooctane and
FT cadaverine."
FT /evidence="ECO:0000269|PubMed:22408253"
FT MUTAGEN 313
FT /note="K->M: Increases acceptance of polyamines lacking a
FT secondary amine."
FT /evidence="ECO:0000269|PubMed:22408253"
FT MUTAGEN 461
FT /note="E->A: Increases relative acceptance of spermine,
FT norspermidine and 1-aminoethyl-1,3-propanediamine."
FT /evidence="ECO:0000269|PubMed:22408253"
FT MUTAGEN 461
FT /note="E->D: Displays selectivity close to that of wild
FT type."
FT /evidence="ECO:0000269|PubMed:22408253"
FT HELIX 5..15
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 17..36
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 64..73
FT /evidence="ECO:0007829|PDB:3TO3"
FT TURN 75..78
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 87..95
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:3TO3"
FT TURN 107..109
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 114..137
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 149..155
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 174..180
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 182..184
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 191..196
FT /evidence="ECO:0007829|PDB:3TO3"
FT TURN 197..199
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 200..203
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 207..218
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 220..232
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 237..239
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 259..263
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 266..272
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 277..279
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 296..299
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 301..305
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 314..332
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 335..339
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 348..354
FT /evidence="ECO:0007829|PDB:3TO3"
FT TURN 360..363
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:3TO3"
FT TURN 373..376
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 382..385
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 386..390
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 401..407
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 409..431
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 439..441
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 442..447
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 450..456
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 459..462
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 464..466
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 467..469
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 484..488
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 493..499
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 501..508
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 509..515
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 516..527
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 531..547
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 550..552
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 553..559
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 564..569
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 571..576
FT /evidence="ECO:0007829|PDB:3TO3"
FT STRAND 584..588
FT /evidence="ECO:0007829|PDB:3TO3"
FT HELIX 590..601
FT /evidence="ECO:0007829|PDB:3TO3"
SQ SEQUENCE 612 AA; 72014 MW; 95997E3AD6861FFD CRC64;
MRMDMYHTKI LKAIESEDYI SVRRRVLRQL VESLIYEGII TPARIEKEEQ ILFLIQGLDE
DNKSVTYECY GRERITFGRI SIDSLIVRVQ DGKQEIQSVA QFLEEVFRVV NVEQTKLDSF
IHELEQTIFK DTIAQYERCN KLKYTQKSYD ELENHLIDGH PYHPSYKARI GFQYRDNFRY
GYEFMRPIKL IWIAAHKKNA TVGYENEVIY DKILKSEVGE RKLEAYKERI HSMGCDPKQY
LFIPVHPWQW ENFIISNYAE DIQDKGIIYL GESADDYCAQ QSMRTLRNVT NPKRPYVKVS
LNILNTSTLR TLKPYSVASA PAISNWLSNV VSQDSYLRDE SRVILLKEFS SVMYDTNKKA
TYGSLGCIWR ESVHHYLGEQ EDAVPFNGLY AKEKDGTPII DAWLNKYGIE NWLRLLIQKA
IIPVIHLVVE HGIALESHGQ NMILVHKEGL PVRIALKDFH EGLEFYRPFL KEMNKCPDFT
KMHKTYANGK MNDFFEMDRI ECLQEMVLDA LFLFNVGELA FVLADKYEWK EESFWMIVVE
EIENHFRKYP HLKDRFESIQ LYTPTFYAEQ LTKRRLYIDV ESLVHEVPNP LYRARQLNIQ
KSVATGGNYA NC
