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
//