PCHF_PSEAE
ID PCHF_PSEAE Reviewed; 1809 AA.
AC Q9HWG4; O85740;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Pyochelin synthase PchF {ECO:0000305};
DE EC=6.2.1.69 {ECO:0000305|PubMed:9846750};
DE AltName: Full=L-cysteine--[L-cysteinyl-carrier protein] ligase {ECO:0000305};
DE AltName: Full=Nonribosomal peptide synthase PchF {ECO:0000305};
GN Name=pchF {ECO:0000303|PubMed:9846750};
GN OrderedLocusNames=PA4225 {ECO:0000312|EMBL:AAG07613.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, PATHWAY, INDUCTION, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=9846750; DOI=10.1099/00221287-144-11-3135;
RA Reimmann C., Serino L., Beyeler M., Haas D.;
RT "Dihydroaeruginoic acid synthetase and pyochelin synthetase, products of
RT the pchEF genes, are induced by extracellular pyochelin in Pseudomonas
RT aeruginosa.";
RL Microbiology 144:3135-3148(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [3]
RP FUNCTION, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=11208777; DOI=10.1128/jb.183.3.813-820.2001;
RA Reimmann C., Patel H.M., Serino L., Barone M., Walsh C.T., Haas D.;
RT "Essential PchG-dependent reduction in pyochelin biosynthesis of
RT Pseudomonas aeruginosa.";
RL J. Bacteriol. 183:813-820(2001).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore pyochelin
CC (PubMed:9846750, PubMed:11208777). Adenylates L-cysteine and loads it
CC onto its peptidyl carrier domain via a thioester linkage to the
CC phosphopanthetheine moiety (By similarity). Then forms a peptide bond
CC between the salicyl-thiazolinyl intermediate bound to the second
CC carrier domain of PchE and the cysteine bound to its own peptidyl
CC carrier domain to form the salicyl-thiazolinyl-cysteinyl-S-PCP2
CC intermediate. It subsequently cyclizes the C-terminal cysteine to form
CC the second thiazoline heterocycle in the salicyl-thiazolinyl-
CC thiazolinyl-S-PCP2 intermediate (By similarity). When this intermediate
CC is released by the action of a thioesterase, it produces the tricyclic
CC acid hydroxyphenyl-thiazolyl-thiazolinyl-carboxylic acid (HPTT-COOH),
CC an advanced intermediate containing the aryl-4,2-bis-heterocyclic
CC skeleton of the bithiazoline class of siderophores (By similarity).
CC {ECO:0000250|UniProtKB:A0A0H2ZGJ4, ECO:0000269|PubMed:11208777,
CC ECO:0000269|PubMed:9846750}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[peptidyl-carrier protein] + L-cysteine = AMP +
CC diphosphate + L-cysteinyl-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:61680, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15906,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:35235,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144926, ChEBI:CHEBI:456215;
CC EC=6.2.1.69; Evidence={ECO:0000305|PubMed:9846750};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61681;
CC Evidence={ECO:0000305|PubMed:9846750};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:11208777,
CC ECO:0000269|PubMed:9846750}.
CC -!- INDUCTION: Expression of the pchEF operon is strictly dependent on the
CC PchR regulator and is induced by extracellular pyochelin, the end
CC product of the pathway. Repressed by Fur and iron.
CC {ECO:0000269|PubMed:9846750}.
CC -!- DOMAIN: Modular protein that contains a condensation/cyclization domain
CC involved in the cyclization of the cysteine, an adenylation domain
CC which activates the cysteine residue into an aminoacyl-AMP ester, a
CC peptidyl carrier protein (PCP2) domain which bears a
CC phosphopantetheinyl arm to attach the activated cysteine and a
CC thioesterase domain (TE) that may release the newly synthesized peptide
CC from the enzyme. {ECO:0000250|UniProtKB:A0A0H2ZGJ4}.
CC -!- DISRUPTION PHENOTYPE: Mutant can still form salicylate and Dha, but is
CC no longer able to synthesize pyochelin. {ECO:0000269|PubMed:9846750}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; AF074705; AAC83657.1; -; Genomic_DNA.
DR EMBL; AE004091; AAG07613.1; -; Genomic_DNA.
DR PIR; C83118; C83118.
DR PIR; T17403; T17403.
DR RefSeq; NP_252915.1; NC_002516.2.
DR RefSeq; WP_003148107.1; NZ_QZFW01000022.1.
DR AlphaFoldDB; Q9HWG4; -.
DR SMR; Q9HWG4; -.
DR STRING; 287.DR97_3686; -.
DR ESTHER; pseae-PCHF; Thioesterase.
DR PaxDb; Q9HWG4; -.
DR PRIDE; Q9HWG4; -.
DR EnsemblBacteria; AAG07613; AAG07613; PA4225.
DR GeneID; 880083; -.
DR KEGG; pae:PA4225; -.
DR PATRIC; fig|208964.12.peg.4426; -.
DR PseudoCAP; PA4225; -.
DR HOGENOM; CLU_000022_2_15_6; -.
DR InParanoid; Q9HWG4; -.
DR OMA; GVACHGY; -.
DR PhylomeDB; Q9HWG4; -.
DR BioCyc; PAER208964:G1FZ6-4298-MON; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000036; F:acyl carrier activity; IBA:GO_Central.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IBA:GO_Central.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.10.1830; -; 1.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 1.
DR Gene3D; 3.40.50.12780; -; 1.
DR Gene3D; 3.40.50.150; -; 1.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020459; AMP-binding.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR041464; TubC_N.
DR InterPro; IPR044894; TubC_N_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR Pfam; PF18563; TubC_N; 1.
DR PRINTS; PR00154; AMPBINDING.
DR SUPFAM; SSF47336; SSF47336; 1.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Ligase; Phosphopantetheine; Phosphoprotein; Reference proteome.
FT CHAIN 1..1809
FT /note="Pyochelin synthase PchF"
FT /id="PRO_0000454828"
FT DOMAIN 1407..1488
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 69..490
FT /note="Condensation/cyclization"
FT /evidence="ECO:0000305"
FT REGION 520..915
FT /note="Adenylation"
FT /evidence="ECO:0000305"
FT REGION 1584..1797
FT /note="Thioesterase"
FT /evidence="ECO:0000305"
FT MOD_RES 1442
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 799..805
FT /note="LFSLGGA -> AVQPGRR (in Ref. 1; AAC83657)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1809 AA; 197084 MW; 39978C86A1BB5F0B CRC64;
MSLGELLETC RSRRIELWSE AGRLRYRAPQ GALDAGLAER LRAEREALLE HLEGGPGWRA
EPDMAHQRFP LTPVQAAYVL GRQAAFDYGG NACQLYAEYD WPADTDPARL EAAWNAMVER
HPMLRAVIED NAWQRVLPEV PWQRLTVHAC AGLDEAAFQA HLERVRERLD HACAALDQWP
VLRPELSIGR DACVLHCSVD FTLVDYASLQ LLLGEWRRRY LDPQWTAEPL EATFRDYVGV
EQRRRQSPAW QRDRDWWLAR LDALPGRPDL PLRVQPDTRS TRFRHFHARL DEAAWQALGA
RAGEHGLSAA GVALAAFAET IGRWSQAPAF CLNLTVLNRP PLHPQLAQVL GDFTALSLLA
VDSRHGDSFV ERARRIGEQM FDDLDHPTFS GVDLLRELAR RRGRGADLMP VVFTSGIGSV
QRLLGDGEAP RAPRYMISQT PQVWLDCQVT DQFGGLEIGW DVRLGLFPEG QAEAMFDDFV
GLLRRLAQSP RAWTDGDATE PVEAPPQALP GSARSIAAGF AERALLTPDA TAIHDAAGSY
SYRQVAQHAS ALRRVLEAHG AGRGRRVAVM LPKSAAQLVA VIGILQAGAA YVPVDIRQPP
LRRQAILASA EVVALVCLES DVPDVGCACV AIDRLAADSA WPPPPAAEVA ADDLAYVIYT
SGSTGTPKGV MLSHAAVSNT LLDINQRYGV DANDRVLGLA ELSFDLSVYD FFGATAAGAQ
VVLPDPARGS DPSHWAELLE RHAITLWNSV PAQGQMLIDY LESEPQRHLP GPRCVLWSGD
WIPVSLPTRW WRRWPDSALF SLGGATEAAI WSIEQPIRPQ HTELASIPYG RALRGQSVEV
LDARGRRCPP GVRGEIHIGG VGLALGYAGD PQRTAERFVR HPDGRRLYRT GDLGRYLADG
SIEFLGREDD QVKIRGHRIE LAELDAALCA HPQVNLAATV VLGETHERSL ASFVTLHAPV
EAGEDPRTAL DAVRQRAAQA LRRDWGSEEG IAAAVAALDR ACLASLAAWL AGSGLFASAT
PLDLATLCQR LGIAEARQRL LRHWLRQLEE GGYLRAEGEG WLGCAERPAQ SPEDAWTAFA
GCAPAALWPA ELVAYLRDSA QSLGEQLAGR ISPAALMFPQ GSARIAEAMY SQGLHAQALH
EAMAEAIAAI VERQPQRRWR LLELGAGTAA ASRTVIARLA PLVQRGAEVD YLFTDVSSYF
LAAARERFAD QPWVRFGRFD MNGDLLDQGV APHSVDILLS SGALNNALDT PALLAGLREL
LSADAWLVIQ ELTREHNEIS VSQSLMMENP RDLRDERRQL FVHTGQWLEW LAAQGGDLAC
GVVPPGSALD LLGYDVLLAR CKTDRARLEP AELLAFVEAR VPRYMLPAQL RVLERLPVTG
NGKIDRKALT GFARQPQADL RHGVAQAPAD ELENALLALW REVLDNPSLG VEQDFFGAGG
DSLLIAQLIA RLRERLESAR RHPFDRLLRW ALSQPTPRGL AERLRSAPEE GRGPALAAAR
GVAPAPAGMS RAPLAEGAVA LDPLVRLVPG EGVPRVLVHE GLGTLLPYRP LLRALGEGRP
LLGLAVHDSD AYLAIPAEHL NACLGRRYAE ALHRAGLREV DLLGYCSGGL VALETAKSLV
QRGVRVRQLD IVSSYRIPYR VDDERLLLFS FAATLGLDTA ALGFPAPERL GQAVQAALAQ
TPERLVAEAL AGLPGLADLV ALRGRVLQAA SGSADAVSVE RDTLYRLFCH SVRASQAEAP
EPYVGALRLF VPDAGNPLVP RYAEALETQW RAAALGACGI HEVPGGHFDC LGEALAQSLS
KPMPEEASR
