ID V9W3Z3_9BACL Unreviewed; 1239 AA.
AC V9W3Z3;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Amino acid adenylation protein {ECO:0000313|EMBL:AHD04335.1};
GN ORFNames=ERIC2_c04880 {ECO:0000313|EMBL:AHD04335.1};
OS Paenibacillus larvae subsp. larvae DSM 25430.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=697284 {ECO:0000313|EMBL:AHD04335.1, ECO:0000313|Proteomes:UP000029431};
RN [1] {ECO:0000313|EMBL:AHD04335.1, ECO:0000313|Proteomes:UP000029431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25430 {ECO:0000313|EMBL:AHD04335.1,
RC ECO:0000313|Proteomes:UP000029431};
RX PubMed=24599066;
RA Djukic M., Brzuszkiewicz E., Funfhaus A., Voss J., Gollnow K., Poppinga L.,
RA Liesegang H., Garcia-Gonzalez E., Genersch E., Daniel R.;
RT "How to Kill the Honey Bee Larva: Genomic Potential and Virulence
RT Mechanisms of Paenibacillus larvae.";
RL PLoS ONE 9:E90914-E90914(2014).
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
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DR EMBL; CP003355; AHD04335.1; -; Genomic_DNA.
DR AlphaFoldDB; V9W3Z3; -.
DR KEGG; plv:ERIC2_c04880; -.
DR PATRIC; fig|697284.3.peg.464; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG3320; Bacteria.
DR HOGENOM; CLU_000022_2_17_9; -.
DR Proteomes; UP000029431; Chromosome.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd05930; A_NRPS; 1.
DR CDD; cd05235; SDR_e1; 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; 3.40.50.720; NAD(P)-binding Rossmann-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; IPR020459; AMP-binding.
DR InterPro; IPR020845; AMP-binding_CS.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR013120; Far_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
DR PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PIRSF; PIRSF001617; Alpha-AR; 3.
DR PRINTS; PR00154; AMPBINDING.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000029431}.
FT DOMAIN 754..828
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1239 AA; 139767 MW; FCA0FF824AAF7F60 CRC64;
MTSKREETMF TVKKQYHSSH QSLPVLQIPL DAARHVRTYK YTQTENSVPS AINRLLADHK
DRQVLLLTAY FSWMYRLSGE KELAAGIEGK SGTLFPLKLS LENIHTFEAL EELIRNQLAG
IPEQSENFEE EALQTDTFFL CHSGFPENEE KGPIISWLVR VNTKGKFSIL IRYDASLLSP
DSVKRFSSYF LTLLQAAGNR PDQRINSVDI LTDEDLNMYQ KLNRTETPYP ENQTIHGMFE
QAASRFPEHL ALASQQEEYT YAALNRRANQ IAHLLLEKEV RKGDFVTIFM DRSLETIISL
LGIMKAGGVY VPVDPDHPEE RNSYIVEDTR SAFILTKQIY ADKARHLSTP ITSVKEIVPI
DSKDLDNYPA DNPGVHVDPD DLAYIIYTSG STGKPKGALI AHRGVVNLGF VVKEQCGISE
REVLTQFATY SFDASVWDTI GALFFGAKLY LLSAEERVSV EEFADAIERT GTTIITILPT
VFFNQLATYL SDEGYTKLKK VKLITVAGEA LYGELVRSVQ RKFGEHIEII NVYGPTECTV
CTTTHKISGY LPEDLANVPI GKPIDNYKIY IVNEDHQLCP LNVPGEIYIS TVGLAKGYLN
QPEKTRQSFI PSPFALNELI YKSGDIARLL KNGTVEYVGR RDSQIKIRGH RIEIGEIEDN
FAKYPDVQDV AVIPKKEPDG QNMLVAYFTS KDQDKLPLSK VKQFLSDRLP SYFIPKYLCQ
LNQLPLSPTG KIDRKKLAGF PHEDAFDKDR NYVAPQTEPQ RLIAKAWEEV LNKKPIGLTD
DFFDIGGDSL DVLHVLALLK PRFTKLRIND FFTYKTVEQL AERAEDLMEE TQGRKNAASF
TNITDLDEHP LYLKNSAGTL KYGVPKHVLL TGATGYLGSH LLYELLTKTD AVIYPIVRKT
SAGTGRSRLQ DILKLYFGEA VLGLAKNRVK VMEGDLEAPG LGLPGENLSL LRQHIDTIVH
SAADVRHFGD AAQFEKTNIF ATKHLADLAM FKKGIRFHHI STMGIPEDLA LSGQWETVLR
KEEFDPDLRV ENVYTQSKLE AEKLLFKASK QGAAITIYRA GNLSCHSESG RFQRNIDSNA
FYRMIKAMLL LEKAPEVNWH VDFTPVDFAS EAIVHLASQP DTANRIFHIC HPEPIRYEQL
LGMIRACGYN VETMAFDEYT NWLLDSSIPK ETEALQLAMA QLEGDGAKDS AYRYGCKETT
AFLNRGRVRC KPVDQAFIQK MILHAVEVGY FPKPRITNK
//