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Database: UniProt
Entry: V9W3Z3_9BACL
LinkDB: V9W3Z3_9BACL
Original site: V9W3Z3_9BACL 
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
//
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