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Database: UniProt
Entry: A0A081BS86_9BACT
LinkDB: A0A081BS86_9BACT
Original site: A0A081BS86_9BACT 
ID   A0A081BS86_9BACT        Unreviewed;      1199 AA.
AC   A0A081BS86;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=NcpB protein {ECO:0000313|EMBL:GAK54267.1};
GN   ORFNames=U14_05546 {ECO:0000313|EMBL:GAK54267.1};
OS   Candidatus Moduliflexus flocculans.
OC   Bacteria; Candidatus Moduliflexota; Candidatus Moduliflexia;
OC   Candidatus Moduliflexales; Candidatus Moduliflexaceae.
OX   NCBI_TaxID=1499966 {ECO:0000313|EMBL:GAK54267.1};
RN   [1] {ECO:0000313|EMBL:GAK54267.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Sekiguchi Y., Ohashi A., Parks D.H., Yamauchi T., Tyson G.W.,
RA   Hugenholtz P.;
RT   "First genomic representation of candidate bacterial phylum KSB3 points to
RT   enhanced environmental sensing as a trigger of wastewater bulking.";
RL   PeerJ 3:e740-e740(2015).
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DR   EMBL; DF820461; GAK54267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A081BS86; -.
DR   STRING; 1499966.U14_05546; -.
DR   HOGENOM; CLU_000022_2_17_0; -.
DR   Proteomes; UP000030700; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   CDD; cd17652; A_NRPS_CmdD_like; 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; IPR020845; AMP-binding_CS.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR013120; Far_NAD-bd.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR009081; PP-bd_ACP.
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; PF00668; Condensation; 1.
DR   Pfam; PF07993; NAD_binding_4; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   PIRSF; PIRSF001617; Alpha-AR; 3.
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.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030700}.
FT   DOMAIN          704..779
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1199 AA;  134941 MW;  F6287886F1865F54 CRC64;
     MLLYRYTGQE DLLIGFPVAN RHAVEFEALL GLFMNTLVLR TDLSGNPTFL ELLARVRSAT
     LTAQEHQELP FERLIAAIYP DRDPSYHPVF QSMFVFENMP MPIFRLSKVT LMPIDIFNHT
     AKFDCSLVLT EKEDELAGQI EYSTDLFTPQ TIERLVNHFH ILLKEIVAHP ERRIAEIPML
     TEAECRLFFQ TEPFEKLPNS SMKCVHQLFE EQVERTPNAI ALVFDEQYLT YQQLNRKANQ
     LAHYLQRHGV EPETLVGICM ERSFEMIIGL LGVLKAGGAY LPLVPTYPQE RLAFMMQDSR
     MLLLLTHTAT YDNLSLDRPG SVVCLNGDWS QFEGESQENP KNNVSANSLA YVIYTSGSTG
     VPKGVLVTHI GIPNLCAAQI LAFRLSEQSR VLQMASFGFD ASVSEIFTTF LAGATLVLMP
     QEKILPGEPL AQTLRETKIS IVTLPPSVLE ILEERNLPDL QTVISAGEAC SAEIIQRWSA
     GRHFINAYGP TEATVCATMN EQVDSIHPSN IGRAIPGVAL YILNSSLQPC PIGVPGELHI
     GGIALARGYL NQPELTAERF IPNPFSPQSG KRLYKTGDLA RFLPDGTIEY LGRIDHQVKI
     RGFRIELGEI EAVLRQQPKI AQSVVIMREH GSRGKHLLAY IVPQSGVTIS TSDVRMSLKR
     SLPDYMIPDV IMVLDKFPLT PNGKIDRLAL PHPEQGTFHE NFVAPRHPIE QILANTWAEI
     LEIEQVGIHD NFFELGGHSL LTMKLMFRVC DIFQVKLPLR MLFEAPTIAE FAKILEAVRG
     VNVEDKLMHI GAVDEVAESQ LDEKIRPESL ELPETRFSNP AIVFLTGATG FLGAFLLAEL
     LQKTKAQVYC LVRAATVEEG WQRLQNTLKK YALWHNGIVQ DRIVPILGDL SLPRFGVSEE
     QFQQLACEID MIYHNGAMVN LVYPYAGLKA ANVDAAKDII RLACVARLKP IHYISTMSVF
     LTAGFAKKRT VYEDTPLDSF DELIQEGYAQ SKWIAEKLLE QAKERNVPVT IYRPGTISGH
     SVTGVWNTDD VVCSVIKGCI QLGKAPYKNI IYTYLTPVDY VSQAIMHLSQ QPTSAGRVFH
     LVNPMPLQWN EIVDWIYDFG YPFERLSYKA WQAALVPLAT ARTQENALSH LLPVYLENEP
     DRYEPQFFDC QRTLDALTGT DITCPSIPSL LETYFANFIR TGFLWKPVRQ DQGTYREEQ
//
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