ID W5TH39_9NOCA Unreviewed; 1317 AA.
AC W5TH39;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:AHH18507.1};
GN ORFNames=NONO_c37200 {ECO:0000313|EMBL:AHH18507.1};
OS Nocardia nova SH22a.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=1415166 {ECO:0000313|EMBL:AHH18507.1, ECO:0000313|Proteomes:UP000019150};
RN [1] {ECO:0000313|EMBL:AHH18507.1, ECO:0000313|Proteomes:UP000019150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH22a {ECO:0000313|EMBL:AHH18507.1};
RX PubMed=24747905;
RA Luo Q., Hiessl S., Poehlein A., Daniel R., Steinbuchel A.;
RT "Insights into the Microbial Degradation of Rubber and Gutta-Percha by
RT Analysis of the Complete Genome of Nocardia nova SH22a.";
RL Appl. Environ. Microbiol. 80:3895-3907(2014).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
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DR EMBL; CP006850; AHH18507.1; -; Genomic_DNA.
DR STRING; 1415166.NONO_c37200; -.
DR KEGG; nno:NONO_c37200; -.
DR PATRIC; fig|1415166.3.peg.3820; -.
DR eggNOG; COG0110; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR HOGENOM; CLU_002751_1_0_11; -.
DR Proteomes; UP000019150; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR CDD; cd05930; A_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 2.160.10.10; Hexapeptide repeat proteins; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
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; IPR042099; ANL_N_sf.
DR InterPro; IPR018357; Hexapep_transf_CS.
DR InterPro; IPR012728; NRPS_C.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR011004; Trimer_LpxA-like_sf.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR02353; NRPS_term_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; PF00550; PP-binding; 1.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF51161; Trimeric LpxA-like enzymes; 3.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000019150};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 663..690
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 850..883
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 903..926
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1101..1121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1127..1151
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 527..601
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1295..1317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1317 AA; 138010 MW; 334FF3B47F50DE57 CRC64;
MIVESDAAAS NRSPVASQAA DLVSPLLRSG TAAPPRTLVD ILADTAHAHP DAAALDDGGQ
VLTYRELLDE IDITVAELRA AGIGRGDRVG VRIPSGTARL YVTILAVLHA GAAYVPVDAD
DPDERAELVF GEAAVAAVAG ADGITPAAGR SESGRDTTES ALEADIRVVP GEDDDAWIIF
TSGSTGTPKG VAVTHRNAAA FVDAEARLFL RETPIGPGDR VLAGLSVAFD ASCEEMWLAW
RHGACLVPAP RALVRSGMDL GPWLVRRGIS IVSTVPTLAA MWPPEALDAV RLLIFGGEAV
PPELAERLAG TGEREVWNTY GPTEATVVAC AAQLTGEPPV RIGLPLDGWD LAVVDADGRP
VAEGESGELV IGGVGLARYL DPAKDAEKYA PMPTLGWRRA YRSGDLVRND SAGLIFLGRA
DDQVKVGGRR IELGELDAAL QNLPGVTAAA AAVRTTAAGT PILIGYLSSS DENFDVAAAR
ELLAGRLPAA LVPRLAVLGE LPVRTSGKVD RNALPWPLPG SDTDPRADLD GTEYWLAGLW
NSVLGAEVSG PDADFFDLGG GSLSAAQLVT ALRERVPRIT VADLYDHPRL GALAELIDAT
APAEETVERI VAPTPRRAQW FQVLASVPLT TLTGLQWLTW LGVITNIASR FGALPWMPGL
SWWWALAGFV LFISPPGRMA ICVAGARLLL HDLRPGTYPR GGSVHLRLWT AVRLAEAAGA
ENLSGAPWMV PFARALGAKI GHGVDLHTLP PVTGMLELGD GCSVEPEVDL AGYWIDGDLV
HIGEIRIGPG AVIGSRSTLL PGAVIGRDAV VEPGSAVFGK VKAGQSWAGS PAVKIGPAEH
RWPGTTPPRA LSWVFVFGVT SMLLSALPVA ALAAGGLLLA WWVRDETTLP GALGHAMAML
PVAALIVLVV FAAVTVVAIR ILSIGLTEGY HPVRSRVGWQ AWATERLTDS ARTFLFPLYA
SLLTPIWLRL LGASVGKNVE ASTVLLLPKF TKVADGAFLA DDTMVAGYEL GGGWMHIGGA
KVGKRAFLGN SGMTAPGRRV PKNGLVAVLS AAPEKAKAGS SWLGSPPVRL RRTAGDSDTS
RTFDPPLRLK LARALVETCR LIPVVLTFGI GLAVLFALAW LASGPGYWLA ALCSGVVLLI
AGAVAGALAV AAKWLIVGRI GAIEHPLWSS FVWRNEVCDA FVETVAAPWF ARAATGTAVM
NIWLRGLGAQ IGRGVWCESY WLPEADLVSL GDGATVERGC VVQTHLFHDR IMSMDTVTLE
PGATLGPHCV ALPAARVGAG ATVGPASLVM RGDTVPPSTR WQGNPIAPWQ DSGHGGK
//
