ID D2NSJ5_ROTMD Unreviewed; 1455 AA.
AC D2NSJ5;
DT 02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT 02-MAR-2010, sequence version 1.
DT 27-MAR-2024, entry version 75.
DE SubName: Full=Non-ribosomal peptide synthetase modules {ECO:0000313|EMBL:BAI64621.1};
GN OrderedLocusNames=RMDY18_07890 {ECO:0000313|EMBL:BAI64621.1};
OS Rothia mucilaginosa (strain DY-18) (Stomatococcus mucilaginosus).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Rothia.
OX NCBI_TaxID=680646 {ECO:0000313|EMBL:BAI64621.1, ECO:0000313|Proteomes:UP000001883};
RN [1] {ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Mashimo C., Sugimori C., Yamanaka T., Leung K.,
RA Fukushima H.;
RT "Complete genome sequence of Rothia mucilaginosa DJ.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAI64621.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64621.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Yoshida M., Fujihira T., Baba T., Tsuji N., Hayashi H.,
RA Sugimori C., Yamanaka T., Mashimo C., Nambu T., Kawai H., Fukushima H.;
RT "Isolation and identification of Rothia mucilaginosa from persistent apical
RT periodontitis lesions.";
RL J Osaka Dent Univ 44:93-98(2010).
RN [3] {ECO:0000313|EMBL:BAI64621.1, ECO:0000313|Proteomes:UP000001883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY-18 {ECO:0000313|EMBL:BAI64621.1,
RC ECO:0000313|Proteomes:UP000001883};
RA Yamane K., Nambu T., Yamanaka T., Mashimo C., Sugimori C., Leung K.-P.,
RA Fukushima H.;
RT "Complete Genome Sequence of Rothia mucilaginosa DY-18: A Clinical Isolate
RT with Dense Meshwork-Like Structures from a Persistent Apical Periodontitis
RT Lesion.";
RL Sequencing 2010:457236-457236(2010).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; AP011540; BAI64621.1; -; Genomic_DNA.
DR SMR; D2NSJ5; -.
DR STRING; 680646.RMDY18_07890; -.
DR KEGG; rmu:RMDY18_07890; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3319; Bacteria.
DR HOGENOM; CLU_000022_2_13_11; -.
DR Proteomes; UP000001883; 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:0008610; P:lipid 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; cd05930; A_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
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; IPR001031; Thioesterase.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00823; PKS_PP; 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:UP000001883}.
FT DOMAIN 1097..1172
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1455 AA; 155118 MW; 5957DEECA1FB0FAF CRC64;
MREATMGVAD TTAPASFGTA SDLRTAANPS AQHSADSPWL PLTTNARGIY FAAAIDPTNP
CYNTAEVLQC PADTDLALLR EAFEQLYREN EGFRVRTRIA DGAASQQILP LEVFLAGIDL
LVDEGELSDT AKAEEENASD LPESALPDSD LPAPVSAWAQ RLLAQPLTTD EGVTVRSAVV
RYGGFLWVYH SFSHVVADGF AAFNGLSRVA AIYRALFAGQ PVPATRRMSL HQLLDADDAA
STAREEDVAF WEASGALEQE DTSLAGRTAS PSARSVRLAF SIDVPTQQAL LDAAKQHAVS
WPVLATAAVG SYLARVGGYP QASFGVPQMN RMFARTLPEA TRALGAASAQ TGCTAVNVLP
VQVAATGSIA ESLHSVKEQY ARNAEHPLAR QEDLERTARN AQSRLFGAQI NVVPFDAVLP
LAAPSKGGSG APVPTARIHN ISAGPVADAT FTLRGMPGRG NSISCEIDMN PALYTAEELE
RHAARLSEWL PAYAAEAQRE DASLNNLGLA TEAELATLRE LTAPALTEHP MEYKTLLDRF
REAVAAHPQA LAVLDSAPAP GEVLTPESER AYAFDRALTY AELDERARAL AAQLLDWGVR
PSDAVGLRVH RGAEQYVALY ALLYAGATYV PVLPDLPAER VGVMMEDAEC SLLLHGPGLQ
PLSAEELNPQ EPARHANLPQ HTLPQLTIEE AVQAPAAEEL PGTKTGLDED AYVLFTSGST
GRPKGVAISH RAIDNRLRWQ QHQIPVGEGD RVLHKTPISF DVHVWELYWP LAEGAAVVIA
APDGHRDPAY LARVIAEQSV TAVHFVPTML SALTSSPAAR RILADAGFGQ DREQPLRYVV
CSGEALQKDQ VQAAGEVLGV YPLNLYGPTE AAVDVTFWET SGDPQRESVP IGEPVWNTGT
LILDPTGHPV PVGVTGELHL SGVQLARGYK NNPQATAAAF VEQAPAGALA LLNGESQRLY
RTGDLACWEI LSDGRAVIGY RGRTDYQIKV RGQRLELGDI EMALAAVEGV SASVALLYRG
LREPALAAVL EVGDVPAERA EQLVEAAREH CAQVLPDYMV PTLWHTLPAL PVSPSGKADR
KLLASLDLTP QTSDAEGPHG LLEQQLCSII ADVLGRERFG VDEDFFASGG HSLAALEVIA
AVEEQLGLSV SIGALFAHPT VQALVASIAG ERGEGAEFAP VLPLREHILT QREHVVTQRE
QPVVPDTTEA PAPLFILPPA GGLGWCYAGY LSHLPAQQGV YALQAEAFSD PQAGFASSLQ
ELAEGYLKLI EKTLAERSLP RRFALMGWSV GGTAAVQVAA LAQAAGAQVE RVILLDAYPS
EQWQGVPAPD EQESFRALLR MGGLPEPAAG EQLDLPGTLE RLQRAGSAMG YLPEEKLGVC
LGSMRASAAL MRGAEQAFFD GDVLLVGVPH EDQPYLDAAG WAAHASSFRS VLLEGTHPDL
VNPARLAEVT GHFAG
//
