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Database: UniProt
Entry: A0A1X7HG96_9BACL
LinkDB: A0A1X7HG96_9BACL
Original site: A0A1X7HG96_9BACL 
ID   A0A1X7HG96_9BACL        Unreviewed;      1347 AA.
AC   A0A1X7HG96;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Phosphopantetheine attachment site {ECO:0000313|EMBL:SMF85062.1};
GN   ORFNames=SAMN05661091_2855 {ECO:0000313|EMBL:SMF85062.1};
OS   Paenibacillus uliginis N3/975.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=1313296 {ECO:0000313|EMBL:SMF85062.1, ECO:0000313|Proteomes:UP000192940};
RN   [1] {ECO:0000313|EMBL:SMF85062.1, ECO:0000313|Proteomes:UP000192940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N3/975 {ECO:0000313|EMBL:SMF85062.1,
RC   ECO:0000313|Proteomes:UP000192940};
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; LT840184; SMF85062.1; -; Genomic_DNA.
DR   STRING; 1313296.SAMN05661091_2855; -.
DR   Proteomes; UP000192940; Chromosome i.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   CDD; cd08953; KR_2_SDR_x; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 1.10.1240.100; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR036736; ACP-like_sf.
DR   InterPro; IPR014031; Ketoacyl_synth_C.
DR   InterPro; IPR014030; Ketoacyl_synth_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR032821; PKS_assoc.
DR   InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR   InterPro; IPR013968; PKS_KR.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR016039; Thiolase-like.
DR   PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF16197; KAsynt_C_assoc; 1.
DR   Pfam; PF00109; ketoacyl-synt; 1.
DR   Pfam; PF02801; Ketoacyl-synt_C; 1.
DR   Pfam; PF08659; KR; 1.
DR   Pfam; PF00550; PP-binding; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SUPFAM; SSF47336; ACP-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 1.
DR   PROSITE; PS52004; KS3_2; 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:UP000192940};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        915..935
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          26..449
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          1220..1295
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   REGION          638..663
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1190..1217
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        638..659
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1347 AA;  150921 MW;  A29000CFEF9E95AE CRC64;
     MDFQSIKLNR KSIAELEDVA FDRTSSQDIA IVGIAVKLPL ADTVEQFANN LKTGRDCVRP
     IPSLRKQDTD LYFKQMGLEP EDLAYGEAAY LDEIDKFDYS FFKLSPREAS LLDPNQRLFL
     ETAWRAIEDA GYGGGKLGGS PTGVYVGYGS DADYLKLIRQ VEPEAVSMSM AGNVRPIIAS
     RLSYLMDLRG PSFIVDSTCS SSLVAVHLAC QAIRNGECDS AIVGGTQLHL IPIREYEVGI
     ESSTSRARTF DDRADGTGTG EGVVAMMLKP LEQAIESRDH IYAVIKSSAL NQDGGSVGIT
     APNAEAQEAV IADAWKRAGI DPETIGYIET HGTGTKLGDP IEVEGLKRAF RRFTDKRQFC
     AIGALKSNIG HLDNTAGIAG LLKAVLSLKN KCIYPTLHFD RPNRVIDFAE SPVYVNDKLM
     EWKSGPHPRR CGVSSFGISG TNCHVILEEA PVERSWMKPQ HDEYRLFVLS AQTVSALETY
     VDASLDYLMH RPSIDFGDLC YTLGTGRGHY RYRIAIAAKS VDEVVDELRS FKTAGFKGMQ
     DRSQGESNSS LYADSIDRLQ SQLEAIRSAA EVVFATYFSS DRMDRMLCAE LGRLYVQGVS
     IPWERLYRQE RRRRLSFPTY PFDRYRCWVN LTDHTSKGRA RHTSAKRNDA YEAARNESHN
     QDQDQSAFYH QRRWLPEPLP QIGRKSHGCE TILILTEDHQ DSSPFVRRWK AVGSKVIEAA
     MGDSFKVVDV TKYIVRDEME DYERLLHDAF DSFNSLGDRS LLIVDLRFAA FGNEDETLEK
     HEQQLEQSIY RLYRLIHALA RRDGHESIAV TLVTSYADEV TAEQPRVRPE QFAMIGLSKA
     AGWENPNLKI RWIDVDEQSD LVESVCSELE VETTEYWTAY RQGKRYVECV DVLRLEEEVS
     SSLQPFFIRS QDINGTYLIT GGLGSIGLLI VSHFVKESKG NIRLALMGRT ALPPRDQWPD
     LEHADQDKKI VRAIRAIREM EDAGAQIEVI QADVSNKEQL SKAITSLRQR HGRIAGIVHA
     AGVSEGNLMS RLSAEELRSV IASKTTGTWL LDHLTRQDKP DFLVLYSSAI TLVGGIGSGP
     YTAGNAYLDG YSAYRNRFGL RTLTINWPAW KETEKDEADE VDESKEMFCL MSQEDGIRAF
     QELLQASEAA PVRQAIVGRW NRGSHLFVLG ELLPFRQSEQ VQQALTRSIT TDKTHAKADH
     RRSAGTANNG TFAAPNKWPT THSEIEEAVA EAWKQVLGYE ELDVHANFFE IGGDSILITR
     VHHYIDEEFP GLTTVADMFS YPTIARITDH LYDVVSDTEE TGETTLESIE ANSFNEAIFA
     MFERVKRGEL SIENAVDLYR GMEVANG
//
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