ID A0A1N7QMM1_9BACT Unreviewed; 1311 AA.
AC A0A1N7QMM1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Tyrocidine synthetase-2 {ECO:0000313|EMBL:SIT23747.1};
DE Flags: Fragment;
GN ORFNames=SAMN05421788_1061 {ECO:0000313|EMBL:SIT23747.1};
OS Filimonas lacunae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Filimonas.
OX NCBI_TaxID=477680 {ECO:0000313|EMBL:SIT23747.1, ECO:0000313|Proteomes:UP000186917};
RN [1] {ECO:0000313|Proteomes:UP000186917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21054 {ECO:0000313|Proteomes:UP000186917};
RA Varghese N., Submissions S.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; FTOR01000006; SIT23747.1; -; Genomic_DNA.
DR STRING; 477680.SAMN05421788_1061; -.
DR Proteomes; UP000186917; Unassembled WGS sequence.
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: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 CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.30.559.30; 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; IPR020459; AMP-binding.
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; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
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; PF13193; AMP-binding_C; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF00550; PP-binding; 1.
DR Pfam; PF00975; Thioesterase; 1.
DR PRINTS; PR00154; AMPBINDING.
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.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000186917}.
FT DOMAIN 996..1071
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:SIT23747.1"
SQ SEQUENCE 1311 AA; 148486 MW; 13FC461A53C3AD22 CRC64;
LEMKLTLNEF FRYPVIRELS AYLSGKDKVG YEAIAAAPVL DYYPLSHAQK RLWILQQLAE
ERQAYNVPKV FYLQGVPDVD RLRHSFELLV QRHDILRTVF RVVNGEVKQH IVRKDLLPDC
FQVVTMLQLR DAGVTSDEFI HKRINKAFDL ENGPLLQVYL VQQQKQAYTL LINMHHIIAD
AWSMKILLSE LVAFYNTPEV LLPLLSIQYK DYAWWEAEYL ESDHGQRHRK FWMETLHGDI
ARIHLPEKAN RPARKTFNGS SCGYQFSNTL TQRLKGMAAD EGTSMFVLLM AAFNALFYRY
LGIDDMVIGT VVAGREREEL LQQVGFYVNT LAVRNRFSGQ DSFIKLLGKV KENVLLALEH
QYYPFDRIVS DLGGAADADR QSLFDIMLVY QNQEEWTEGA LEIEGMTLQP GKGELEGSKF
DISFVVSERE TGLHFYIEYN TDIYEGAFML QLMGHLKLLL ESVLQLPEKP IAYLDYLPGE
EHQLLLQFNS TAFAEALHFP AIQCYFENQA VHFPDNAAII SGDRVWSYRQ VNEITNRLAH
WIRSEYSDRV DRVIAFVADR SEWQVMLMLG ILKSGAAFLP IDPTNPSERI VFMLNDAMPL
LVITDTEEVT WLAAVTSKVI GLEVIIDQLP GYAATNPVLL NTPEDMAYVI YTSGSTGRPK
GVVIEHRGTI NLAHDQVRRF AITPADRSLQ FATVSFDAAI YEIFMALFSA AGVVVVAQEV
INQPVAFVQY LQQCGVTIAT LPPVYLASLG KQVLQPLRIL VTAGEAPGKE YAAYHSTYLD
YYNAYGPTEY SVCTSIYQVA GNEVIIPIGK PLINTQVYIL DQHQQLLPQG FWGEITVSGK
GIARGYLNRP DLTKEKFIDH PFIPGEKLYR TGDIGRWTPE GDIVFAGRRD NLVKIRGYRV
ELAEIEQVLL LHPDVSTVAV TYRKEAGSRD VLSAYIESDA SNDIAALKWW LAQKLPYYMI
PGYFFFMKAI PLTASGKINY GALPVELTGD AVEQVSPVNA IEVLLLEIWQ EVLQLKNIST
EDDFFAIGGH SILAMRFMSL LWERMNKTVS IRDLVKYPTI RSLAEFINRD SSDKGLLLPL
NRVSGNDLPL FMIPPVVGSS TVFTALAAAL EEKEIRCYGL QYRGFDYDVP FDESMQVMAE
SFAAEIISAG TGQKIYVLGY SMGALLAVET VRSLERKGYT AGLILLDKDP SAGWSDFDVR
NAKEEDALLE IFQLHFSHQQ QVEFKDMDRL QRLLAHNISL LQSYRTVGKI KADILALEAL
DSSKQNKMRK WKTRTSGSFE HQLCEGNHFS LIQDSNIPTL TDFISQFVIN H
//