PCHE_PSEAB
ID PCHE_PSEAB Reviewed; 1438 AA.
AC A0A0H2ZGB9;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 16-SEP-2015, sequence version 1.
DT 03-AUG-2022, entry version 34.
DE RecName: Full=Pyochelin synthase PchE {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 PchE {ECO:0000305};
GN Name=pchE {ECO:0000303|PubMed:10555976};
GN OrderedLocusNames=PA14_09270 {ECO:0000312|EMBL:ABJ13499.1};
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, AND DOMAIN.
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). Accepts salicylate activated by PchD at the first
CC peptidyl carrier domain (ArCP), and activates and fixes one molecule of
CC cysteine at the second peptidyl carrier domain (PCP1) via a thioester
CC linkage to the phosphopanthetheine moiety (PubMed:10555976). Then
CC catalyzes the condensation reaction between the salicylate bound to the
CC first site and the cysteine bound to the second site, and the
CC cyclization of the cysteine to form the salicyl-thiazolinyl-S-PCP1
CC intermediate at the second site (PubMed:10555976). When this
CC intermediate is released by the action of a thioesterase, it produces
CC the antifungal antibiotic dihydroaeruginoic acid (Dha or hydroxyphenyl-
CC thiazolinyl-carboxylate) (By similarity).
CC {ECO:0000250|UniProtKB:G3XCV2, 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=110 uM for L-cysteine {ECO:0000269|PubMed:10555976};
CC Note=kcat is 38 min(-1) with L-cysteine as substrate.
CC {ECO:0000269|PubMed:10555976};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000269|PubMed:10555976}.
CC -!- PATHWAY: Antifungal biosynthesis. {ECO:0000250|UniProtKB:G3XCV2}.
CC -!- DOMAIN: Modular protein that contains an aryl carrier protein (ArCP)
CC domain which bears a phosphopantetheinyl arm to attach the activated
CC salicylic acid, a condensation/cyclization domain involved in the
CC cyclization of the cysteine, an adenylation domain which activates the
CC cysteine residue into an aminoacyl-AMP ester and a peptidyl carrier
CC protein (PCP1) domain which bears a phosphopantetheinyl arm to attach
CC the activated cysteine. {ECO:0000305|PubMed:10555976}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; CP000438; ABJ13499.1; -; Genomic_DNA.
DR RefSeq; WP_003137469.1; NZ_CP034244.1.
DR EnsemblBacteria; ABJ13499; ABJ13499; PA14_09270.
DR KEGG; pau:PA14_09270; -.
DR HOGENOM; CLU_000022_40_2_6; -.
DR OMA; CAPESIR; -.
DR BioCyc; PAER208963:G1G74-773-MON; -.
DR Proteomes; UP000000653; Chromosome.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 2.
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 InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF53335; SSF53335; 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 Antibiotic biosynthesis; Ligase; Phosphopantetheine; Phosphoprotein;
KW Repeat.
FT CHAIN 1..1438
FT /note="Pyochelin synthase PchE"
FT /id="PRO_0000454825"
FT DOMAIN 6..85
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1350..1425
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 136..442
FT /note="Condensation/cyclization"
FT /evidence="ECO:0000305"
FT REGION 563..950
FT /note="Adenylation"
FT /evidence="ECO:0000305"
FT MOD_RES 46
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1385
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1438 AA; 156534 MW; 68FCE7142F4191A7 CRC64;
MDLPPDSRTA LRDWLTEQLA DLLGEPLADV RALADDDDLL GCGLDSIRLM YLQERLRARG
STLDFAQLAQ RPCLGAWLDL LACADRLSAP ATVALPTVQD RDQPFELSSV QQAYWLGRGA
GEVLGNVSCH AFLEFRTRDV DPQRLAAAAE CVRQRHPMLR ARFFDGRQQI LPTPPLSCFD
LQDWRTLQVD EAERDWQALR DWRAHECLAV ERGQVFLLGL VRMPGGEDRL WLSLDLLAAD
VESLRLLLAE LGVAYLAPER LAEPPALHFA DYLARRAAQR AEAAARARDY WLERLPRLPD
APALPLACAP ESIRQPRTRR LAFQLSAGES RRLERLAAQH GVTLSSVFGC AFALVLARWS
ESAEFLLNVP LFDRHADDPR IGEVIADFTT LLLLECRMQA GVSFAEAVKS FQRNLHGAID
HAAFPALEVL REARRQGQPR SAPVVFASNL GEEGFVPAAF RDAFGDLHDM LSQTPQVWLD
HQLYRVGDGI LLAWDSVVGL FPEGLPETMF EAYVGLLQRL CDSTWEQPAD LPLPWAQQAR
RALLNGQPAC ATARTLHRDF FLRAAEAPDA DALLYRDQRV TRGELAERAL RIAGGLREAG
VRPGDAVEVS LPRGPQQVAA VFGVLAAGAC YVPLDIDQPP ARRRLIEEAA GVCLAITEED
DPQALPPRLD VQRLLRGPAL AAPVPLAPQA SAYVIYTSGS TGVPKGVEVS HAAAINTIDA
LLDLLRVDAA DRLLAVSALD FDLSVFDLFG GLGAGASLVL PAQEQARDAA AWAEAIQRHA
VSLWNSAPAL LEMALSLPAS QADYRSLRAV LLSGDWVALD LPGRLRPRCA EGCRLHVLGG
ATEAGIWSNL QSVDTVPPHW RSIPYGRPLP GQAYRVVDAH GRDVPDLVVG ELWIGGASLA
RGYRNDPELS ARRFVHDAQG RWYRTGDRGR YWDDGTLEFL GRVDQQVKVR GQRIELGEVE
AALCAQAGVE SACAAVLGGG VASLGAVLVP RLAPRAEGSM ELPAAQPFAG LAEAEAVLTR
EILGALLEAP LELDDGLRRR WLDWLADSAA SALPPLDEAL RRLGWQAAGL TAMGNALRGL
LAGEQAPAAL LLDPWLAPQA VAARLPDGRE ALARLLEALP TPAAGERLRV AVLDTRAGLW
LDQGMASLLR PGLELTLFER SRVLLDAAAT RLPERIVVQA LDDGLLPAEH LGRYDRVISF
AALHAYAASR EGLALAAALL RPQGRLLLVD LLCESPLALL GAALLDDRPL RLAELPSLLA
DLAAAGLAPR CLWRSERIAL VEALAPGLGL DAAALQAGLE QRLPQAMRPE RLWCLPSLPL
NGNGKVDRRR LAESMTRALG ECRDEPSAEE PLEAHEQALA ECWEAVLKRP VRRREASFFS
LGGDSLLATR LLAGIRERFG VRLGMADFYR QPTLAGLARH LQAQTVEIEE TQLEEGVL
