ID A0A0Q4VDB4_9MICO Unreviewed; 1311 AA.
AC A0A0Q4VDB4;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Amino acid adenylation protein {ECO:0000313|EMBL:KQO64669.1};
GN ORFNames=ASF23_00170 {ECO:0000313|EMBL:KQO64669.1};
OS Curtobacterium sp. Leaf261.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Curtobacterium.
OX NCBI_TaxID=1736311 {ECO:0000313|EMBL:KQO64669.1, ECO:0000313|Proteomes:UP000050821};
RN [1] {ECO:0000313|EMBL:KQO64669.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO64669.1,
RC ECO:0000313|Proteomes:UP000050821};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQO64669.1, ECO:0000313|Proteomes:UP000050821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf261 {ECO:0000313|EMBL:KQO64669.1,
RC ECO:0000313|Proteomes:UP000050821};
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:KQO64669.1}.
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DR EMBL; LMMJ01000001; KQO64669.1; -; Genomic_DNA.
DR RefSeq; WP_055947313.1; NZ_LMMJ01000001.1.
DR STRING; 1736311.ASF23_00170; -.
DR OrthoDB; 2472181at2; -.
DR Proteomes; UP000050821; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0044249; P:cellular biosynthetic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 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; 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; IPR042099; ANL_N_sf.
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; 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.
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:UP000050821};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 848..877
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 897..922
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1093..1117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 1123..1147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 524..598
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1311 AA; 136609 MW; B9F654A2ECE176C9 CRC64;
MAAGSSDGPT DGAAGTVLAD HAQPELSAGS RAPRPRTLLD VLTSTAEEHP DALALEDPEG
GISYRRLLAL VRHGADDLAS RGVGVGDRVG IRISSGTRTL SVAVLSVLAA GAAYVPVDAD
DPEERADLVF GEAGVVGVIG DGGVLRARDG SRMPVLDDAV DTARPGPGLD DDAWIIFTSG
STGVPKGVAV THRSAAAFVD AEARMFLQRE PIGSGDRVLA GLSVAFDASC EEMWLAWGHG
ACLVPAPRAL VRSGVDLGPW LIAHGITIVS TVPTLAALWP DDALELVRLV IFGGEACPPE
LAARITARGR EVWNTYGPTE ATVVACGAPL DGGTPIRIGL PLDGWDLAVV DASGARVSEG
EVGELIIGGV GLARYLDPAK DAEKYASFPQ LGWDRAYRSG DLVRYEAAGL VFQGRADDQV
KLGGRRIELG EVDAALRSLD GVAGGAAVVQ RTAAGNQVLV GYVAVSGEPA DFDRAAATAR
LREDLPAALV PLLAVVDDLP TRTSGKVDRA ALPWPLDDAP GESAVLPPTV AWIAERWSAI
LGAPVTSPDD DFFAHGGGSL TAAQLVSAIR ERFPNTTVAD VYDHPRIGAL AEAIDVDGGE
TAAEARSVLP VPPATGFAMA LLGLPLHILV GLRILTFVAI ANDVLQATTL PFLPTVPWQV
LVVGIVVFVS PPGKMAITVA CARVLLLGVR AGAHPRGGSV HIRVWLAEQI AHLVDGPSLS
GAPWIAYYAR ALGAKIGPGV DLHTLPPVTG MLTIGGHAAV EPEVDLVGHW VDGDVFRIGA
MHIGSDAIVR SRSTLLPGAR VGAGAEIEPG SAVAGRVPAG ERWAGSPAHR VGSARRDKLG
RPPRGRGWLV AYGVGSLVAA GLPVVGVAVG VLVVVALVGR APDLGAAART AAAAVPLATI
AAGATYALLV VVAVRLLGIG LAEGRHPVRS RIGWQVWSTE RILDAARTLL FPLYASLVTP
VWLRLLGARV GADAEISTVL LVPKLTAIAP GAFLADDTMV ATYELGGGRM RIGRSKVGRR
AFLGNSGMTA GGRSVPREAL VAVLSAVPRK AKRGSSWLGS PPVRLRRATA EFDESRTFSP
PTRLRVARGL WELLRLLPVM VSGWIALAVV VVLEWVWTEV GLGWAILLSG VVLVLAGAVA
AAITTAAKWA FVGRIRAEEH PLWSSFVWRN EVQDTFVEMV ARPWFATNAA GTPVLAAWLR
TLGASIGRGV WCESYWLPEA DLVRLGDGAT VNRGCVVQTH LFHDRVMQLD GVRLDAGATL
GPHSVILPAA AIDDGATVGP ASLVMRGERV PAGSVWSGNP ITPWVRPPWQ R
//
