PHSC_STRVT
ID PHSC_STRVT Reviewed; 1086 AA.
AC D9XF47; Q4JFF2; Q5IW58;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=Phosphinothricin tripeptide synthase PhsC {ECO:0000305};
DE Short=PTT synthase PhsC {ECO:0000305};
DE EC=6.2.1.67 {ECO:0000269|PubMed:16251301};
DE AltName: Full=L-alanine--[L-alanyl-carrier protein] ligase {ECO:0000305};
DE AltName: Full=Nonribosomal peptide synthase PhsC {ECO:0000305};
DE AltName: Full=Phosphinothricin tripeptide synthetase II {ECO:0000303|PubMed:16251301};
DE Short=PTT synthetase II {ECO:0000303|PubMed:16251301};
GN Name=phsC {ECO:0000303|PubMed:15574905};
GN ORFNames=SSQG_01044 {ECO:0000312|EMBL:EFL30526.1};
OS Streptomyces viridochromogenes (strain DSM 40736 / JCM 4977 / BCRC 1201 /
OS Tue 494).
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=591159;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX PubMed=15574905; DOI=10.1128/aem.70.12.7093-7102.2004;
RA Schwartz D., Berger S., Heinzelmann E., Muschko K., Welzel K.,
RA Wohlleben W.;
RT "Biosynthetic gene cluster of the herbicide phosphinothricin tripeptide
RT from Streptomyces viridochromogenes Tu494.";
RL Appl. Environ. Microbiol. 70:7093-7102(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX PubMed=15616300; DOI=10.1128/aac.49.1.230-240.2005;
RA Blodgett J.A., Zhang J.K., Metcalf W.W.;
RT "Molecular cloning, sequence analysis, and heterologous expression of the
RT phosphinothricin tripeptide biosynthetic gene cluster from Streptomyces
RT viridochromogenes DSM 40736.";
RL Antimicrob. Agents Chemother. 49:230-240(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces viridochromogenes strain DSM 40736.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, DOMAIN, AND DISRUPTION PHENOTYPE.
RC STRAIN=DSM 40736 / JCM 4977 / BCRC 1201 / Tue 494;
RX PubMed=16251301; DOI=10.1128/aac.49.11.4598-4607.2005;
RA Schwartz D., Grammel N., Heinzelmann E., Keller U., Wohlleben W.;
RT "Phosphinothricin tripeptide synthetases in Streptomyces viridochromogenes
RT Tue494.";
RL Antimicrob. Agents Chemother. 49:4598-4607(2005).
CC -!- FUNCTION: Involved in the biosynthesis of the antibiotic
CC phosphinothricin tripeptide (PTT), which has bactericidal, fungicidal
CC and herbicidal properties (PubMed:16251301). Adenylates L-alanine and
CC loads it onto a peptidyl carrier domain via a thioester linkage to the
CC phosphopanthetheine moiety (PubMed:16251301). Shows weaker activity
CC with aminobutyric acid and L-serine (PubMed:16251301).
CC {ECO:0000269|PubMed:16251301}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + holo-[peptidyl-carrier protein] + L-alanine = AMP +
CC diphosphate + L-alanyl-[peptidyl-carrier protein];
CC Xref=Rhea:RHEA:61800, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:15938,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:64479, ChEBI:CHEBI:144958, ChEBI:CHEBI:456215;
CC EC=6.2.1.67; Evidence={ECO:0000269|PubMed:16251301};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:61801;
CC Evidence={ECO:0000269|PubMed:16251301};
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC -!- PATHWAY: Antibiotic biosynthesis. {ECO:0000305|PubMed:16251301}.
CC -!- DOMAIN: Modular protein that contains a condensation domain, an
CC adenylation domain which activates the alanine residue into an
CC aminoacyl-AMP ester and a peptidyl carrier protein domain which bears a
CC phosphopantetheinyl arm to attach the activated amino acid.
CC {ECO:0000305|PubMed:16251301}.
CC -!- DISRUPTION PHENOTYPE: Mutant cannot produce PTT. PhsC cannot take on
CC the function of PhsB and vice versa. {ECO:0000269|PubMed:16251301}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; X65195; CAJ14039.1; -; Genomic_DNA.
DR EMBL; AY632421; AAU00074.1; -; Genomic_DNA.
DR EMBL; GG657757; EFL30526.1; -; Genomic_DNA.
DR RefSeq; WP_003988641.1; NZ_GG657757.1.
DR STRING; 591159.ACEZ01000045_gene2953; -.
DR EnsemblBacteria; EFL30526; EFL30526; SSQG_01044.
DR KEGG; ag:CAJ14039; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_4_11; -.
DR OrthoDB; 572620at2; -.
DR BioCyc; MetaCyc:MON-15059; -.
DR BRENDA; 6.2.1.67; 6116.
DR Proteomes; UP000004184; Unassembled WGS sequence.
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:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0030639; P:polyketide biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
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 Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF47336; SSF47336; 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 Reference proteome.
FT CHAIN 1..1086
FT /note="Phosphinothricin tripeptide synthase PhsC"
FT /id="PRO_0000454848"
FT DOMAIN 1006..1081
FT /note="Carrier"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 22..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..484
FT /note="Condensation"
FT /evidence="ECO:0000305"
FT REGION 510..901
FT /note="Adenylation"
FT /evidence="ECO:0000305"
FT REGION 983..1007
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1041
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 288
FT /note="G -> V (in Ref. 1; CAJ14039)"
FT /evidence="ECO:0000305"
FT CONFLICT 673..674
FT /note="GI -> AF (in Ref. 1; CAJ14039)"
FT /evidence="ECO:0000305"
FT CONFLICT 739
FT /note="R -> P (in Ref. 1; CAJ14039)"
FT /evidence="ECO:0000305"
FT CONFLICT 946
FT /note="E -> K (in Ref. 1; CAJ14039)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1086 AA; 118822 MW; A9156029565AD7A7 CRC64;
MEDLQTRIAA LSPKQRALFE SRLRAAAAPG PDPAIPRRPD DDGPVPLSFA QHRLWFLDQL
EPGRPVYNVS ASLRIGRPVT TEAVRDALGA LTRRHEVLRT VFPADGGEPR QHIADSLTPP
LTETDLRALP DSARAAAALR LCAEDKQRPF DLSSGPLLRC LLLRLRDDDA LLFLTFHHTV
FDGWSIGLLR RDLTALLHAA ETGTDAGLPP LPIQYADFAD WQRRMLDEKR LGELLGYWRE
RIRGAPPVID LPFDRPRPAV ATTEGARRRF ALPAELTTAL RDLAARSGAT PFMTMLTVFA
ALLHRWSGER DMVIGTPVAN RARPELDDLI GFFANTLAMR VRIEPGMSFG DLLAQVRQTV
VEALARQDLP FERLVDEART ERTLTHNPLF QVAFVMEDGR DASELDTLLP ERARDTHTPD
SAKFDLTLVL TDRESTYTGY FEYNTALFEP VTIDRLGERL ALLARSVAAD PGWELAALPV
LTRDEIRHLK EVNAPVADDP RHHRTLHGVL EDSARRHPDH TAVEAPDRQL TYRELDEAAN
RLAHHLLALG VRPEQPVGVA LDGTADAIVA TFAVLKAGAV LLPLDPEYPA ERLEHILRRS
GATLLLTQRS LAGRFAGNDV TTVLLDDDAT RAALADGPAD RPGLPIAPDR LAYVIFTSGS
TGVPKGVMVP HRGIGSLTRS AEQFAQTPDS RVLRFASPSF DVSLLELLMT FDAGATLVLE
PRALLVPGED LARLIRERRV STVLLSPSAL STLTAGELPG LRTVVMAGEA ATLELAQQWC
DGRDVFNGYG PTEATVLATI ARCAPDRVPP LGRPVAGYTV HVLDDTLRPV PFGRQGELFL
GGVGLARGYL DQPDVTADRF LPDPSGTEPG ARLYRTGDVV RWGADGELEF LGRTDHQVKL
RGFRIELGEI ETRLEDHPGV RTAVVLVRGE GSDRRLAGYA VRAPGEERPT AAGLRQWLRD
RLPGYMVPEL FLVLDALPTS PNGKLDREAL PDPLAQSGDT AGNRPPLLDP VEERISGIWQ
EVLGIAPPGS ADNFFEVGGN SLSATRIIAR VNQAFGVRLP VRSLFVEPTL SGLARSVSAE
RAEELP
