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PLTF_PSEF5
ID   PLTF_PSEF5              Reviewed;         498 AA.
AC   Q4KCY5;
DT   11-DEC-2019, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
DE   RecName: Full=L-proline--[L-prolyl-carrier protein] ligase {ECO:0000305};
DE            EC=6.2.1.53 {ECO:0000269|PubMed:11880032};
DE   AltName: Full=L-prolyl-AMP ligase {ECO:0000303|PubMed:11880032};
GN   Name=pltF {ECO:0000312|EMBL:AAY92064.1};
GN   OrderedLocusNames=PFL_2792 {ECO:0000312|EMBL:AAY92064.1};
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=11880032; DOI=10.1016/s1074-5521(02)00100-x;
RA   Thomas M.G., Burkart M.D., Walsh C.T.;
RT   "Conversion of L-proline to pyrrolyl-2-carboxyl-S-PCP during
RT   undecylprodigiosin and pyoluteorin biosynthesis.";
RL   Chem. Biol. 9:171-184(2002).
CC   -!- FUNCTION: Involved in the biosynthesis of pyoluteorin. Catalyzes the
CC       conversion of L-proline to L-prolyl-AMP and the transfer of the L-
CC       prolyl group to acyl carrier protein PltL.
CC       {ECO:0000269|PubMed:11880032}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + holo-[peptidyl-carrier protein] + L-proline = AMP +
CC         diphosphate + L-prolyl-[peptidyl-carrier protein];
CC         Xref=Rhea:RHEA:11656, Rhea:RHEA-COMP:11480, Rhea:RHEA-COMP:14109,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:64479, ChEBI:CHEBI:138622, ChEBI:CHEBI:456215;
CC         EC=6.2.1.53; Evidence={ECO:0000269|PubMed:11880032};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000305}.
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DR   EMBL; CP000076; AAY92064.1; -; Genomic_DNA.
DR   RefSeq; WP_011061084.1; NC_004129.6.
DR   PDB; 6O6E; X-ray; 2.14 A; B=1-498.
DR   PDBsum; 6O6E; -.
DR   AlphaFoldDB; Q4KCY5; -.
DR   SMR; Q4KCY5; -.
DR   STRING; 220664.PFL_2792; -.
DR   DNASU; 3478039; -.
DR   EnsemblBacteria; AAY92064; AAY92064; PFL_2792.
DR   KEGG; pfl:PFL_2792; -.
DR   PATRIC; fig|220664.5.peg.2848; -.
DR   eggNOG; COG1020; Bacteria.
DR   HOGENOM; CLU_000022_2_12_6; -.
DR   OMA; RTLYPIG; -.
DR   OrthoDB; 377638at2; -.
DR   BioCyc; MetaCyc:MON-20313; -.
DR   BRENDA; 6.2.1.53; 5121.
DR   Proteomes; UP000008540; Chromosome.
DR   GO; GO:0005524; F:ATP binding; ISS:JCVI.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.12780; -; 1.
DR   InterPro; IPR010071; AA_adenyl_domain.
DR   InterPro; IPR025110; AMP-bd_C.
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   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   PRINTS; PR00154; AMPBINDING.
DR   TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Antibiotic biosynthesis; ATP-binding; Ligase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..498
FT                   /note="L-proline--[L-prolyl-carrier protein] ligase"
FT                   /id="PRO_0000448663"
FT   HELIX           4..14
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          18..22
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          27..29
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           30..47
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          54..60
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           63..74
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          78..81
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           88..98
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          101..105
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           110..115
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   TURN            117..120
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          121..127
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           135..137
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          154..161
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          169..174
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           175..189
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          196..199
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           207..217
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          221..224
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           227..229
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           233..242
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          246..250
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           252..261
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   TURN            264..266
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          274..277
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           284..293
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   TURN            294..296
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          297..303
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   TURN            306..308
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          312..316
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          330..332
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          337..341
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          354..360
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          365..367
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          375..385
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          391..403
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          406..409
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           410..418
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          424..433
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           434..436
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          438..444
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           453..461
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           466..468
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          471..475
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   STRAND          485..487
FT                   /evidence="ECO:0007829|PDB:6O6E"
FT   HELIX           489..498
FT                   /evidence="ECO:0007829|PDB:6O6E"
SQ   SEQUENCE   498 AA;  54537 MW;  0A219EED5E35FE84 CRC64;
     MKLLHERMMH SLARYPRQTA VVDEQDALSY EALELRIREF VAMLCALGVG QGQRILLWAH
     KSVDLVAVMQ AALRLGVVYV PVDPLSPVSR LEKIAGDSQA VLVLCTAARL EELAGSALAQ
     VRSVVLDDPA SAGYWRNIDT GSSVVPTLAI QPDDLAYILY TSGSTGVPKG VALSHGNALA
     FVDWACERYC FQPGERFANH APLHFDLSVL DIYCALNVGA TVCLVPESIA FSPRLLTDFI
     RQHEISIWYS VPSVLMMMMQ DGDLLSDIQD TLRVLLFAGE PFPVKHLRDL RAAYADVRLA
     NLFGPTETNV CTAFEVGAID PERVLPVPIG TAASGNQVWA QKPDGSRCAV GEEGELVVQG
     PTVMLGYFAK PAQEGPYKTG DMVRQRPDGN YEYLGRRDDM LKVRGNRIER GEVEAALLAH
     PQVSEAAVLV VGEGMNAQLW GVLVAHTRDA LSLIDLKRHC AQRLPRYMII DKVLCLDALP
     RNANGKVDRF ALARQVEG
 
 
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