ID A0A2W2KHF8_9ACTN Unreviewed; 1486 AA.
AC A0A2W2KHF8;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:PZG88165.1};
DE Flags: Fragment;
GN ORFNames=C1I97_32060 {ECO:0000313|EMBL:PZG88165.1};
OS Streptomyces sp. NTH33.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1735453 {ECO:0000313|EMBL:PZG88165.1, ECO:0000313|Proteomes:UP000248559};
RN [1] {ECO:0000313|EMBL:PZG88165.1, ECO:0000313|Proteomes:UP000248559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NTH33 {ECO:0000313|EMBL:PZG88165.1,
RC ECO:0000313|Proteomes:UP000248559};
RA Sahin N., Ay H., Saygin H.;
RT "Draft genome sequence of Streptomyces sp. NTH33.";
RL Submitted (JAN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PZG88165.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; POTZ01000526; PZG88165.1; -; Genomic_DNA.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000248559; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProt.
DR GO; GO:0008610; P:lipid biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR CDD; cd17652; A_NRPS_CmdD_like; 1.
DR CDD; cd19534; E_NRPS; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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_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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR45398; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR PANTHER; PTHR45398:SF1; ENZYME, PUTATIVE (JCVI)-RELATED; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 2.
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; SSF52777; CoA-dependent acyltransferases; 4.
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:UP000248559}.
FT DOMAIN 958..1032
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 933..963
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1415..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1423..1438
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PZG88165.1"
FT NON_TER 1486
FT /evidence="ECO:0000313|EMBL:PZG88165.1"
SQ SEQUENCE 1486 AA; 159502 MW; 2B109BCD089AB3D9 CRC64;
VPRDTPAPMS YAQQRLWFLE EFAPGSGEYV TALALRLRGR LDVPALTAAL RALVERHEAL
RTTFDTVDGH GVQIVHPAPD VPLTLHDLSG TAQTDRAARL EELLEAERAR TFDLRRGPLL
HAGLIRLTGD EHVLTLTLHH IVTDGWSTGV LTGDLAHFYR AELGSADGQL PPLPVSYADY
AHWQRGNGTD EHLAYWKEHL AGLETLDLPT DRPRPAVRTH GGATVRLVLP RGTTRRLVQV
GRDRQATLFS TLVAAAQTYL ARLTGGRDIT VGTVTSGRDR AETQNLVGFF VNTLVLRSRV
EPDRPFPEFL TEVRGTVLDA FAHQEAPFER VVDEVQPVRD TSRTPLFQVM VVLQNAPAAD
LDLPGIEVTG VDTDLRHAAF DLTLEFAETP AGELHGLLTY NTDLFDAATA ERMADQLGTL
LTAVADDPDR PLGALPLATA ETLKAVLDQG RGTARPVPAA TLPELFERQA ARTPDAVALA
DADGRELTYA EVERAANRLA HRLIARGVGP ERVVALALPR GAGTAVAQLA VAKAGGAFLP
VDPDYPEQRR EFMLRDADAW LVLDDPAAVR DADGPDTAPT DADRTAALTV AHPAYVIYTS
GSSGTPKGVT VTHSGLAAFA AAAADRYDAG PGDRVLQFAS PSFDASVLEL CVSLLSGATL
VTGEEGPLVG ERLAQVLAER RVSHTLIPPA ALATVAPGTS DALPHLRTLI VGAEACPAAL
VERWAPGRRM INSYGPTEAT VVATWTGPLA PGTGAPPIGR PAGATRVHVL DAALRPVPPG
VTGELYVAGP GLARGYLNRP GLTASRFVAD PFGAPGERMY RTGDLARWDA SGELRFAGRA
DDQVKLRGFR IEPGEIESAL RRSPRVRDAV VTVRGGGTDP DGRSGGRLVA HVVPAEGATQ
ELPVPELRDH LAGLLPPHMV PSAFVPLERL PLTPNGKTDR GALPEPGPTH TAAGPRTAPR
TDTERRIARI WADVLGVADV GAHDNFFHLG GDSILSMQVV SRLRRDGLHL ATRDLFTHQT
VAELATVVTD APRHSGDGPV SGDVPLTPIQ EWFLTSPRAS HSHFNQSLLL ELGTTPDAAA
LETALNALLD HHDALRMRFT QDEDGWRQFN PPPSDTDRDR LLDRHDLSGL TSAEADAAME
RAADDLHTGF DLARGPLLRA ALFTGDAGRP ALLLLVAHHL VVDAVSWRIL RDDLEAAYRQ
AVQGEPVAPG ERTTSFRGWA RGLAAHVAAG ALDDELPYWE RAVNAESLPA EAPAGPETGP
VDTLTVELDE ADTAALLRAA PTAYRTRVND VLLAALALAL ARWTGREEVR LDLEGHGRED
VLDDVDLSRT VGWFTTVHPV ALRVPEPDGP GPARDWRTLV KSVRRQLRAV PGNGLGFGAL
RTFGPPEVRR RLGGAAHGQV VFNYLGQWDA RPENPGDGLV RAEHGSFGRH HDPRDSGSHP
LEVVGAVQGG RLSFTWHHRP ALHATDTVRR VADDFAEALR HIAHCA
//
