ID D2UB21_XANAP Unreviewed; 1349 AA.
AC D2UB21;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Probable non-ribosomal peptide synthetase protein {ECO:0000313|EMBL:CBA14904.1};
GN OrderedLocusNames=XALc_0364 {ECO:0000313|EMBL:CBA14904.1};
OS Xanthomonas albilineans (strain GPE PC73 / CFBP 7063).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=380358 {ECO:0000313|EMBL:CBA14904.1, ECO:0000313|Proteomes:UP000001890};
RN [1] {ECO:0000313|EMBL:CBA14904.1, ECO:0000313|Proteomes:UP000001890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GPE PC73 / CFBP 7063 {ECO:0000313|Proteomes:UP000001890};
RX PubMed=20017926; DOI=10.1186/1471-2164-10-616;
RA Pieretti I., Royer M., Barbe V., Carrere S., Koebnik R., Cociancich S.,
RA Couloux A., Darrasse A., Gouzy J., Jacques M.A., Lauber E., Manceau C.,
RA Mangenot S., Poussier S., Segurens B., Szurek B., Verdier V., Arlat M.,
RA Rott P.;
RT "The complete genome sequence of Xanthomonas albilineans provides new
RT insights into the reductive genome evolution of the xylem-limited
RT Xanthomonadaceae.";
RL BMC Genomics 10:616-616(2009).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
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DR EMBL; FP565176; CBA14904.1; -; Genomic_DNA.
DR STRING; 380358.XALC_0364; -.
DR KEGG; xal:XALC_0364; -.
DR eggNOG; COG1020; Bacteria.
DR OMA; YRGEAML; -.
DR Proteomes; UP000001890; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound 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 CDD; cd12116; A_NRPS_Ta1_like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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_com.
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; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF13; ENTEROBACTIN SYNTHASE COMPONENT F; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
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 Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001890}.
FT DOMAIN 954..1029
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1311..1349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1321..1339
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1349 AA; 148146 MW; 516EC79218A99FDF CRC64;
MHADTPSSFP LTRAQRGLWV GSKLQVDKML MLSEALELFG PLDPTLLLQA NRQITREFDV
LRLCIHEQNG LPEQIVLPEY PGELQYLDFS DEPAPRAAAE RWVGDQLGKR ENLRDGPLWF
CVVFRLGQDH HLWVQYTSHL VMDGFTGTML AQRLASLYNA YAFGQEPEPA AYGSVLELVT
LEQEYRASDR YRRDREYWMQ QLSNLPPAVT LAKPGEQNSA GLLRATGEFS PETVLRLRAL
GAAHGASLPQ TLIALVAAYY HRYTGAEDLV MAMPVTGRVG ARYRQVPGLA ANAIYLRLTM
RPNQPFHALF PHVSSVVRHG LRHQQYRVED VRRDLGMFAN MQRIARLAVN IEAFDYGLRF
GEAQAVPHNL CNGLADDLTI FCYERGNGMA LRFDLDANPA LYDREELAEH CRRLSLLADA
ILDAPERPLA LLDILGTQER CRLLWECNAT AMPLPIMATL PHQLLERYAS MPAGIVVQCD
ERTLDDAQVC ELAARIAARW IADGIKPGDV IAVALPRSEQ LLLVLLAVMW SGAAYLPLDP
DGPLVRNRHM LDDAAAIGLV CEPVLRDTLL LDGMVWLDPC PADLPAPIAP LATPEGTAYV
LYTSGSTGIP KGVEISHRSL LNFLFAMRHD LGLRPRDRML AVTTVTFDIA GLELYLPLLV
GARVVIAQGA ITHDPRGLAR LIAQAQVSVI QATPSLWRIL LANDDLPLDK VHALVGGEAL
GAELATRLLA RVGRLTQLYG PTESTIWSTI MPLQLTDAPH PPIGRPIANT RVYVLDPQQQ
LLPTGAVGEL YIGGAGVAKG YRGKPQLTSE RFVCDPFVGD GSRMYRTGDQ VRLRPDGVLE
FIGRIDDQLK IRGHRIEPRE IENALQQHPQ VAQAVVVGHR DHDGTMQLLA YVVALPEQSV
EVDALRQYLQ ACLPSAMLPS RWMSLPALPL TATGKLDRKA LPVPDAPPPR EHVPPRDPIE
QQLAAMVEDI LGINGIGVHD SFFELGVDSL GAAQMAARFP QMFGIELPLV TLLNEPTIAG
VAEVIRRNAQ LHSDPLASAL TLREGEVGTP ALFCIHPVMG MSWSYATLLS QLDPRWPVVL
LQSPGLADSS YRPDSIEAIA HDYLARMRSV QPHGPYRLVG WSLGGLIAHA IAAELRAAGE
LVELLALLDS YPLPPQDAQA DDMISIPAAL RVLDVELAPG TPLPTTMAEL AKVLCDHYGL
LSFPLARQLL EQQHDLVLNI GELIQHHLHL ACHHRPSAID VDVLFVEATR RPDIGMDATD
LIDHRPQVWQ ELVRSLRVEA FDTDHYGILS LAHVGRLAKL LQASVALPTR GSVLDSGSTP
TPTPTPTPTP TPTPTPTPTP TSDGVAEYA
//