ID A0A0Q9K102_9MICO Unreviewed; 1314 AA.
AC A0A0Q9K102;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE SubName: Full=Amino acid adenylation protein {ECO:0000313|EMBL:KRE31299.1};
GN ORFNames=ASG80_02285 {ECO:0000313|EMBL:KRE31299.1};
OS Agromyces sp. Soil535.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1736390 {ECO:0000313|EMBL:KRE31299.1, ECO:0000313|Proteomes:UP000051793};
RN [1] {ECO:0000313|Proteomes:UP000051793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil535 {ECO:0000313|Proteomes:UP000051793};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRE31299.1, ECO:0000313|Proteomes:UP000051793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Soil535 {ECO:0000313|EMBL:KRE31299.1,
RC ECO:0000313|Proteomes:UP000051793};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KRE31299.1}.
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DR EMBL; LMRW01000001; KRE31299.1; -; Genomic_DNA.
DR RefSeq; WP_056728014.1; NZ_LMRW01000001.1.
DR STRING; 1736390.ASG80_02285; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000051793; Unassembled WGS sequence.
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 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 656..684
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 846..876
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 888..918
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1090..1113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1119..1144
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 516..590
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1314 AA; 138427 MW; 02A1B9697DC860CF CRC64;
MTADVPGILD RSALAAAPRT LVDVLRETTH AHPDASALED AAGALSYREL MARVVRTAVR
LHHEGVRRGD RVGIRMPSGS RELYVAILGV MAAGAAYVPV DADDPDERAR LVFGEADVRG
VVSGGGVFEP NGGTESDAPP AGLFDGTPPH PSTHVIPVPT PPELDDDAWI IFTSGSTGTP
KGVAVRHRSA AAFVDAEAKL FLQDAPLGPG DRVLAGLSVA FDASCEEMWL AWRHGACLVP
APRSLVRSGM DLGPWMVTHG ITVVSTVPTL AALWPAEAIE NVRLLIFGGE AVPPELAARL
VSPEREVWNT YGPTEATVVA CAALLDGVGP VRIGVPLDGW ALAVVDPDGR PVGEGEVGEL
IIAGAGLARY LDAEKDAAKY SPMPTLAWER AYRSGDLVVF DPDGLLFQGR VDDQVKVGGR
RIELGEIEAA LQALPGVTGA AAAVRRTEAG NQVLVGYLAA DGEFDRVAAR ARLAEELPAA
LVPLLAVVDE LPTRTSGKVD RDALPWPLPG VVPDAAGLGA SAAWLAELWQ AVLGVPVSEP
DASFFDLGGG SLAAAQLVSR IRARDPEFTV ADIYDRPRLG AMADEVEARV SDTAGSDAAT
FRQPVPTPRG TQWVQTLAGV PLFILSGARW LLYLLTATTI LTAVSADFAF LPTVPIWVLI
VGLALFATPF GRMAIAVVGA RVLLAGLEPG DYPRGGAVHL RMWLADQIAH QVDAVGLSGA
PWVTNYARAL GARIGQDVDL HTLPPVTGML TIGDRAAVEP EVDLAGTWID GDVVRIGRVR
IGAGSTIGAR STLLPGARIG KRAEIAPGSA VFGRVPSGQR WAGSPAERVG PAHITTDEPP
RPRRWLFAYG LSSLLLSLLP IAAFAAGGAV IAAGMAGSAT LGEAALRALA WLVPATLVAG
VAFAGLVVIA VRLLAIGLGE GRHPVRSRVG WQAWTTERLM DASRTILFPL YSSLFTPVWL
RLLGAEVGRD VEASTVLLIP SMTTIDDHAF LADDTMVASY ELQGGWMRLE GARIGKRAFL
GNSGIAAAGH RLARDTLVAV LSVAPAKSKP GTSWLGSPPM RLRRSALEVD ESRTYRPSSR
LRIARTLWEL CRIVPVFVTC AIGLGVLFTL AALTSAFGAV VALLVSGVVM LAAGAVAAIA
STIAKWVFVG RIRAGEHPLW SSFVWRTEVS DTFVEMVAAP WFAQAAAGTP ALAVWLRTLG
ARIGRGVWCD SYWLPEADLV TLGDGSTVNR GCVVQTHLFH DRIMSMDQVT LEPGATLGPH
SVILPAARIG AHATVGPASL VMRGEVVPVG SRWSGNPIGP WRVVRFADYH VQVR
//
