PHSB_STRVT
ID PHSB_STRVT Reviewed; 1189 AA.
AC D9XF49; Q4JFF4; Q5IW60;
DT 23-FEB-2022, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 1.
DT 03-AUG-2022, entry version 62.
DE RecName: Full=Phosphinothricin tripeptide synthase PhsB {ECO:0000305};
DE Short=PTT synthase PhsB {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 PhsB {ECO:0000305};
DE AltName: Full=Phosphinothricin tripeptide synthetase III {ECO:0000303|PubMed:16251301};
DE Short=PTT synthetase III {ECO:0000303|PubMed:16251301};
GN Name=phsB {ECO:0000303|PubMed:15574905};
GN ORFNames=SSQG_01046 {ECO:0000312|EMBL:EFL30528.1};
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 first peptidyl carrier protein
CC domain which bears a phosphopantetheinyl arm to attach the activated
CC amino acid, a condensation domain, an adenylation domain which
CC activates the alanine residue into an aminoacyl-AMP ester and a second
CC peptidyl carrier protein domain. {ECO:0000305|PubMed:16251301}.
CC -!- DISRUPTION PHENOTYPE: Mutant cannot produce PTT. PhsB cannot take on
CC the function of PhsC and vice versa. {ECO:0000269|PubMed:16251301}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; X65195; CAJ14037.1; -; Genomic_DNA.
DR EMBL; AY632421; AAU00073.1; -; Genomic_DNA.
DR EMBL; GG657757; EFL30528.1; -; Genomic_DNA.
DR RefSeq; WP_003988643.1; NZ_GG657757.1.
DR STRING; 591159.ACEZ01000045_gene2955; -.
DR EnsemblBacteria; EFL30528; EFL30528; SSQG_01046.
DR KEGG; ag:CAJ14037; -.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_000022_2_4_11; -.
DR BioCyc; MetaCyc:MON-15058; -.
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; -; 2.
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; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Ligase; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat.
FT CHAIN 1..1189
FT /note="Phosphinothricin tripeptide synthase PhsB"
FT /id="PRO_0000454847"
FT DOMAIN 5..80
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1076..1151
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 75..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..541
FT /note="Condensation"
FT /evidence="ECO:0000305"
FT REGION 454..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..969
FT /note="Adenylation"
FT /evidence="ECO:0000305"
FT REGION 1045..1081
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..97
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 40
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1111
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 157
FT /note="V -> S (in Ref. 1; CAJ14037)"
FT /evidence="ECO:0000305"
FT CONFLICT 743
FT /note="R -> P (in Ref. 1; CAJ14037)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1189 AA; 129117 MW; 007D935E2407AE0A CRC64;
MTAPQTDDVV TGRIAAIWAG LLDRPEIGID DNVFRLGASS VMAVRAAARI REALDTPLPL
RDVFESPSPA ALAKRIRASR STAPTASGPP RTAPVDSTAT APLTFQQEPM WLFDRMQPGN
ATYTIHFALR HEGHLDLGVL DRCVRDVVRR HAVLRTVFPS VDDRPAQQVL DRAHIPLGES
DLRALPEAER PVAAARIAAR EAQAPFDLST GPMLRVRVLH LSDTRQRLLL TMPHIVTDAW
SDDILVRELN HLYRAHTDGI APALPPLPVQ YHDWAARQRA ELAGTEAELL DWWRHHLAGV
PPLLELPADR PRAAVKRHRG GRLLFDIPES VTRRLEGLAK DEGTTPYAVL LAGFAALLHR
LTGQDDLLVG SPVAGRTHTE TEGLVGLFVN TVAVRCDVAG RPSFLELVRR TRRTVVESFA
RQELPFHRLV EELAPVRSPA YTPLVQVMLA LQNTPDRDGR EPGEGPFARE ESGGDTGSAM
FDLTLFVTGS ASGMRGEWEY DSDLFDRERV AELGPQLVTL LDAALDRTDL PVALLPLQEP
AARDRMVQAW NDTADVLPGG PDADSLPALL SAQAHRTPDA VALRTDDGAE LTYRQLHLRA
DRLARRLLSY GLAPESVVAV ACERSFEMVV ALLAVLKAGC AYLPIDPGDP AERTAYLLRD
SGARVLLTLH RHTANLPDAD GTTVVTLDEP DPSGDMQDTT SALPGIAPGQ LAYLIYTSGS
TGRPKGVLNE HGPVCNRIRW GMRAFPPGPG TIVLQKTPIH FDVSVWEMFW TLATGATLVL
ARPDGHRDPQ YLAGRLVEEG VTDVHFVPSM LAAFLDVGAL PEGHSLRRVF CSGEALSPGL
RDRLFARLPH VELHNLYGPT EAAIEVTHWR CRPGEPTVPI GRPIANARCY VLDAELNPVP
PGVPGELWLG GVPVARGYHG RADLTAERFL PDPYGPAGSR MYRSGDLARW RRDGVLEYLG
REDGQVKLRG QRLELGEIEA TLAGHAEVAD VVVDVRGTGP QDRRLVAYVR PARPGRDEQL
RTTLRELAAA RLPAYMRPSS YVTLDRVPLT PSGKTDRKAL PDPAAGEQPR SGRGAAPGTP
AERELAGIWA ELLGAGEVGG DDNFFEIGGH SLLAARMTGR ASTAFGVDLP VSLAFEHPVL
RDFALAVVTA QAATDSAATE RLLAELEALA DTELEALPDE DGPDGRSGE
