PCHF_PSEAB
ID PCHF_PSEAB Reviewed; 1809 AA.
AC A0A0H2ZGJ4;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 35.
DE RecName: Full=Pyochelin synthase PchF {ECO:0000305};
DE EC=6.2.1.69 {ECO:0000269|PubMed:10555976};
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:10555976};
GN OrderedLocusNames=PA14_09280 {ECO:0000312|EMBL:ABJ13498.1};
OS Pseudomonas aeruginosa (strain UCBPP-PA14).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCBPP-PA14;
RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G.,
RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT combinatorial.";
RL Genome Biol. 7:R90.1-R90.14(2006).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, DOMAIN, AND MUTAGENESIS OF 1606-CYS-SER-1607.
RC STRAIN=UCBPP-PA14;
RX PubMed=10555976; DOI=10.1021/bi991787c;
RA Quadri L.E., Keating T.A., Patel H.M., Walsh C.T.;
RT "Assembly of the Pseudomonas aeruginosa nonribosomal peptide siderophore
RT pyochelin: In vitro reconstitution of aryl-4, 2-bisthiazoline synthetase
RT activity from PchD, PchE, and PchF.";
RL Biochemistry 38:14941-14954(1999).
CC -!- FUNCTION: Involved in the biosynthesis of the siderophore pyochelin
CC (PubMed:10555976). Adenylates L-cysteine and loads it onto its peptidyl
CC carrier domain via a thioester linkage to the phosphopanthetheine
CC moiety (PubMed:10555976). Then forms a peptide bond between the
CC salicyl-thiazolinyl intermediate bound to the second carrier domain of
CC PchE and the cysteine bound to its own peptidyl carrier domain to form
CC the salicyl-thiazolinyl-cysteinyl-S-PCP2 intermediate. It subsequently
CC cyclizes the C-terminal cysteine to form the second thiazoline
CC heterocycle in the salicyl-thiazolinyl-thiazolinyl-S-PCP2 intermediate
CC (PubMed:10555976). When this intermediate is released by the action of
CC a thioesterase, it produces the tricyclic acid hydroxyphenyl-thiazolyl-
CC thiazolinyl-carboxylic acid (HPTT-COOH), an advanced intermediate
CC containing the aryl-4,2-bis-heterocyclic skeleton of the bithiazoline
CC class of siderophores (PubMed:10555976). {ECO:0000269|PubMed:10555976}.
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:0000269|PubMed:10555976};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61681;
CC Evidence={ECO:0000269|PubMed:10555976};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000269|PubMed:10555976};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=537 uM for L-cysteine {ECO:0000269|PubMed:10555976};
CC Note=kcat is 415 min(-1) with L-cysteine as substrate.
CC {ECO:0000269|PubMed:10555976};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:10555976}.
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:0000305|PubMed:10555976}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000438; ABJ13498.1; -; Genomic_DNA.
DR RefSeq; WP_011666540.1; NC_008463.1.
DR EnsemblBacteria; ABJ13498; ABJ13498; PA14_09280.
DR KEGG; pau:PA14_09280; -.
DR HOGENOM; CLU_000022_2_15_6; -.
DR OMA; GVACHGY; -.
DR BioCyc; PAER208963:G1G74-774-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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; 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; 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 1: Evidence at protein level;
KW Ligase; Phosphopantetheine; Phosphoprotein.
FT CHAIN 1..1809
FT /note="Pyochelin synthase PchF"
FT /id="PRO_0000454827"
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 MUTAGEN 1606..1607
FT /note="CS->AA: Fails to release HPTT-COOH."
FT /evidence="ECO:0000269|PubMed:10555976"
SQ SEQUENCE 1809 AA; 197109 MW; 9FB6F39B1726D6E4 CRC64;
MSLGELLETC RSRRIELWSE AGRLRYRAPQ GALDAGLAER LRAEREALLE HLEGGPGWRA
EPDLAHQRFP LTPVQAAYVL GRQAAFDYGG NACQLYAEYD WPADTDPARL EAAWNAMVER
HPMLRAVIED NAWQRVLPEV PWQRLTVHAC AGLDEAAFQA HLERVRERLD HACAALDQWP
VLRPELSIGR DDCVLHCSVD FTLVDYASLQ LLLGEWRRRY LDPQWTAEPL EATFRDYVGV
EQRRRQSPAW QRDRDWWLAR LDALPGRPDL PLRAQPDTRS 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 TVIHDAAGSY
SYRQVAQHAS ALRRVLEAHG AGRGRRVAVM LPKSAAQLVA VIGILQAGAA YVPVDIRQPP
LRRQAILASP EVVAWVCLES DVPNAGCACV 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 ASFVTLHAPA
EAGEDPRTAL DTVRQRAAQA LRRDWGSEEG IAAAVAALDR ACLASLAAWL AGSGLFASAT
PLDFATLCQR LGIAEARQRL LRHWLRQLEE GGYLRAEGEG WLGCAERPAQ SPEDAWTAFA
GCAPAALWPA ELVAYLRDSA QSLGEQLAGR ISPAALMFPQ GSARIAEAMY SQGLHAQALH
EAMAEAIAAI VERQPQRRWR LLELGAGTAA ASRAVIARLA PLVQRGTEVD YLFTDVSSYF
LAAARERFAD QPWVRFGRFD MNGDLLDQGV APHSVDILLS SGALNNALDT PALLAGLREL
LSADAWLVIQ ELTREHNEIS VSQSLMMENP RDLRDERRQL FVHTGQWLEW LAAQGGDLAC
GVVPPGSALD LLGYDVLLAR CKTDRARLEP AELLAFVEAR VPRYMLPAQL RVLERLPVTG
NGKIDRKALT GFARQPQADL RHGVAQAPAD ELESALLALW REVLDNPSLG VEQDFFGAGG
DSLLIAQLIA RLRERLESAR RHPFDRLLRW ALSQPTPRGL AERLRSAPEE GRGPALAAAR
GVAPAQTGMS RAPLAEGAVA LDPLVRLVPG EGVPRVLVHE GLGTLLPYRP LLRALGEGRP
LLGLAVHDSD AYLAIPAEYL NACLGRRYAE ALHGAGLREV DLLGYCSGGL VALETAKSLL
QRGVRVRQLD IVSSYRIPYR VDDERLLLFS FAATLGLDTA ALGFPAPERL GQAVQAALAQ
TPERLGAEAL AGLPGLADLV ALRGRVLQAA SGSADAASVE RDTLYRLFCH SVRASQAEAL
EPYVGALRLF VPDAGNPLVP RYAEALETQW RAAALGACGI HEVPGGHFDC LGEALAQSLS
KPMPEEASQ
