ID E0I749_9BACL Unreviewed; 1088 AA.
AC E0I749;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Amino acid adenylation domain protein {ECO:0000313|EMBL:EFM11865.1};
GN ORFNames=PaecuDRAFT_1473 {ECO:0000313|EMBL:EFM11865.1};
OS Paenibacillus curdlanolyticus YK9.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=717606 {ECO:0000313|EMBL:EFM11865.1, ECO:0000313|Proteomes:UP000005387};
RN [1] {ECO:0000313|EMBL:EFM11865.1, ECO:0000313|Proteomes:UP000005387}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YK9 {ECO:0000313|EMBL:EFM11865.1,
RC ECO:0000313|Proteomes:UP000005387};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L.,
RA Pitluck S., Land M.L., Hauser L., Chang Y.-J., Jeffries C., Anderson I.J.,
RA Johnson E., Loganathan U., Mulhopadhyay B., Kyrpides N., Woyke T.J.;
RT "The draft genome of Paenibacillus curdlanolyticus YK9.";
RL Submitted (JUL-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; AEDD01000003; EFM11865.1; -; Genomic_DNA.
DR RefSeq; WP_006037484.1; NZ_AEDD01000003.1.
DR AlphaFoldDB; E0I749; -.
DR STRING; 717606.PaecuDRAFT_1473; -.
DR eggNOG; COG1020; Bacteria.
DR Proteomes; UP000005387; 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:UniProtKB-KW.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd19543; DCL_NRPS; 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; 3.30.559.10; 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; IPR036736; ACP-like_sf.
DR InterPro; IPR025110; AMP-bd_C.
DR InterPro; IPR045851; AMP-bd_C_sf.
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; IPR009081; PP-bd_ACP.
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 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; 2.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005387}.
FT DOMAIN 980..1056
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT COILED 1061..1088
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1088 AA; 123965 MW; 9544727C5E413517 CRC64;
MFNKNVENIY ELSPMQMGML FHSLYAPNSG LYIQQFQAVL NGTVDVEKLS CAWQSVIAKN
AILRTAFFWE NLEKPLQVTF KQVDVSIREV DLTSKTEGEQ ATELEELLSS DLHSDFILSH
APLMRFHLIR LKDERNMFIW THHHILLDGW SVAQLFKEVF DVYEALVKEE EPVFQKRKPF
VDYIEWLQKN AAEDDGHFWH EYLSGFEMPN RLPGEIRTRL PVQPDACNFA VCEKTWSRES
TEKLIQCAKS HQLTLNTIIQ GVWALAIHAY SGDEDIVFGV TVAGRPPSLS GIESMLGLFI
NTLPLRVRID RQSSVGEWLK TIQHQMISLH EYEHTPLHEI QKKSEVAKGP TLFESIVVYE
NYPVSEIPRA SGHGLLIERS QFEETTNFKI TNSVAVSANR ELTFQMKFNK HEIAESVCTA
VMEYIDTLLD YFGNEGMGVP LSHIPKVSAV VQEFYLEQAA KTTDYSDDRC FHQLFEDAVN
QTPDRTAIVC EEQTLTYREL NERANRLARF LKQLGVQNET LVGVHADRNV SLFISLLGIL
KAGGTFVPLD PAHPAERNGR VLEEGGITYL LVDSNDAVDA SANCKVINIS DLQIEQYAPD
NFDEPLSASQ LCYAIFTSGT TGTPKGVLVT HSNLVNAAYA WLEEYRLSEF DVKLLQLASC
AFDVFMGDVA RTFVSGGTLI VCPNAVKLDL PRLYEWVDRH EITIVESTPA LLVPFMEYVH
DQRLPMKSLQ VLILGSDYLA AADYKQLIQR YGHHMRIINS YGVTEATVDS SYFEIRSLEQ
WHESGESHVP IGKPMPNTYY YILDEQLRLV PIGAIGELYI GGRGISRGYL NRTELTQQSF
VRDPFQPDKR LYKTGDLARW REDGIVEFLG REDHQIKIRG YRVELGEIEN ALLEHEAIVR
AAVFYYAEKS SLCAYVVCTK DTSRESVLFD LRRRLPEYMI PHSIEFMETL PLTPNGKVDR
KALPTPGDER GADDESQLVE PLNDIEDQLL EVWKKLLGIQ RISTDQSFFD LGGNSLLILK
LFNEINRLFP NANVSVSDLF SYHTIRQLSK YIRSKHETDD LDLLLLQLEK GEIDLEAAQS
KLQLISRQ
//
