ID   FAA22_MYCBO             Reviewed;         705 AA.
AC   Q7TXK7; A0A1R3Y2P5; X2BM70;
DT   05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 108.
DE   RecName: Full=p-hydroxybenzoic acid--AMP ligase FadD22;
DE            Short=p-HB--AMP ligase FadD22;
DE            EC=6.2.1.50 {ECO:0000269|PubMed:25561717};
DE   AltName: Full=p-hydroxybenzoic acid-AMP synthetase;
DE            Short=p-HB-AMP synthetase;
GN   Name=fadD22; OrderedLocusNames=BQ2027_MB2972C;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA   Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA   Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA   Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA   Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA   Robbe-Austerman S., Gordon S.V.;
RT   "Updated reference genome sequence and annotation of Mycobacterium bovis
RT   AF2122/97.";
RL   Genome Announc. 5:E00157-E00157(2017).
RN   [3]
RP   FUNCTION IN THE BIOSYNTHESIS OF PHENOLPHTHIOCEROL, REACTION MECHANISM, AND
RP   DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=18158259; DOI=10.1016/j.chembiol.2007.11.010;
RA   Ferreras J.A., Stirrett K.L., Lu X., Ryu J.S., Soll C.E., Tan D.S.,
RA   Quadri L.E.;
RT   "Mycobacterial phenolic glycolipid virulence factor biosynthesis: mechanism
RT   and small-molecule inhibition of polyketide chain initiation.";
RL   Chem. Biol. 15:51-61(2008).
RN   [4]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=25561717; DOI=10.1128/jb.02546-14;
RA   Vergnolle O., Chavadi S.S., Edupuganti U.R., Mohandas P., Chan C., Zeng J.,
RA   Kopylov M., Angelo N.G., Warren J.D., Soll C.E., Quadri L.E.;
RT   "Biosynthesis of cell envelope-associated phenolic glycolipids in
RT   Mycobacterium marinum.";
RL   J. Bacteriol. 197:1040-1050(2015).
CC   -!- FUNCTION: Catalyzes the adenylation of p-hydroxybenzoic acid (pHBA) to
CC       form p-hydroxybenzoic acid-AMP (pHBA-AMP), which is converted directly
CC       to p-hydroxybenzoyl-S-FadD22 (pHBA-S-FAdD22) thioester intermediate in
CC       a CoA-independent manner by attack of the phosphopantetheine thiol of
CC       FadD22. This intermediate primes the biosynthesis of the
CC       phenolphthiocerol (PPOL) by presenting the pHBA starter unit for
CC       elongation by Pks15/1. PPOL is an important intermediate in the
CC       biosynthesis of phenolic glycolipid (mycosid B).
CC       {ECO:0000269|PubMed:18158259, ECO:0000269|PubMed:25561717}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-hydroxybenzoate + ATP + holo-[4-hydroxyphenylalkanoate
CC         synthase] = 4-hydroxyphenyl-[4-hydroxyphenylalkanoate synthase] + AMP
CC         + diphosphate; Xref=Rhea:RHEA:54696, Rhea:RHEA-COMP:12684, Rhea:RHEA-
CC         COMP:13969, ChEBI:CHEBI:17879, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:138321, ChEBI:CHEBI:456215;
CC         EC=6.2.1.50; Evidence={ECO:0000269|PubMed:25561717};
CC   -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC   -!- DISRUPTION PHENOTYPE: Disruption of fadD22 abolishes the production of
CC       phenolphthioceroL. {ECO:0000269|PubMed:18158259}.
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; LT708304; SIU01594.1; -; Genomic_DNA.
DR   RefSeq; NP_856617.1; NC_002945.3.
DR   RefSeq; WP_003414884.1; NC_002945.4.
DR   AlphaFoldDB; Q7TXK7; -.
DR   SMR; Q7TXK7; -.
DR   EnsemblBacteria; SIU01594; SIU01594; BQ2027_MB2972C.
DR   PATRIC; fig|233413.5.peg.3264; -.
DR   OMA; PLRDYNA; -.
DR   BioCyc; MetaCyc:MON-19623; -.
DR   UniPathway; UPA00094; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0016874; F:ligase activity; IMP:UniProtKB.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0071766; P:Actinobacterium-type cell wall biogenesis; IMP:UniProtKB.
DR   GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0008610; P:lipid biosynthetic process; IMP:UniProtKB.
DR   Gene3D; 1.10.1200.10; -; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; SSF47336; 1.
DR   PROSITE; PS50075; CARRIER; 1.
PE   1: Evidence at protein level;
KW   Fatty acid metabolism; Ligase; Lipid metabolism; Phosphopantetheine;
KW   Phosphoprotein.
FT   CHAIN           1..705
FT                   /note="p-hydroxybenzoic acid--AMP ligase FadD22"
FT                   /id="PRO_0000406351"
FT   DOMAIN          541..619
FT                   /note="Carrier"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT   MOD_RES         579
FT                   /note="O-(pantetheine 4'-phosphoryl)serine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ   SEQUENCE   705 AA;  75198 MW;  600F2D0EABFDF1DC CRC64;
     MRNGNLAGLL AEQASEAGWY DRPAFYAADV VTHGQIHDGA ARLGEVLRNR GLSSGDRVLL
     CLPDSPDLVQ LLLACLARGV MAFLANPELH RDDHALAARN TEPALVVTSD ALRDRFQPSR
     VAEAAELMSE AARVAPGGYE PMGGDALAYA TYTSGTTGPP KAAIHRHADP LTFVDAMCRK
     ALRLTPEDTG LCSARMYFAY GLGNSVWFPL ATGGSAVINS APVTPEAAAI LSARFGPSVL
     YGVPNFFARV IDSCSPDSFR SLRCVVSAGE ALELGLAERL MEFFGGIPIL DGIGSTEVGQ
     TFVSNRVDEW RLGTLGRVLP PYEIRVVAPD GTTAGPGVEG DLWVRGPAIA KGYWNRPDSP
     VANEGWLDTR DRVCIDSDGW VTYRCRADDT EVIGGVNVDP REVERLIIED EAVAEAAVVA
     VRESTGASTL QAFLVATSGA TIDGSVMRDL HRGLLNRLSA FKVPHRFAVV DRLPRTPNGK
     LVRGALRKQS PTKPIWELSL TEPGSGVRAQ RDDLSASNMT IAGGNDGGAT LRERLVALRQ
     ERQRLVVDAV CAEAAKMLGE PDPWSVDQDL AFSELGFDSQ MTVTLCKRLA AVTGLRLPET
     VGWDYGSISG LAQYLEAELA GGHGRLKSAG PVNSGATGLW AIEEQLNKVE ELVAVIADGE
     KQRVADRLRA LLGTIAGSEA GLGKLIQAAS TPDEIFQLID SELGK