ID A0A1W1XD41_9CLOT Unreviewed; 3064 AA.
AC A0A1W1XD41;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Acyl transferase domain-containing protein {ECO:0000313|EMBL:SMC21807.1};
GN ORFNames=SAMN02745134_01456 {ECO:0000313|EMBL:SMC21807.1};
OS Clostridium acidisoli DSM 12555.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121291 {ECO:0000313|EMBL:SMC21807.1, ECO:0000313|Proteomes:UP000192468};
RN [1] {ECO:0000313|EMBL:SMC21807.1, ECO:0000313|Proteomes:UP000192468}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12555 {ECO:0000313|EMBL:SMC21807.1,
RC ECO:0000313|Proteomes:UP000192468};
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.
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004789}.
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DR EMBL; FWXH01000003; SMC21807.1; -; Genomic_DNA.
DR STRING; 1121291.SAMN02745134_01456; -.
DR OrthoDB; 9765680at2; -.
DR Proteomes; UP000192468; Unassembled WGS sequence.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:InterPro.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd00833; PKS; 2.
DR Gene3D; 1.10.1240.100; -; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.70.250; Malonyl-CoA ACP transacylase, ACP-binding; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR049490; C883_1060-like_KR_N.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
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; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF21394; Beta-ketacyl_N; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 2.
DR Pfam; PF02801; Ketoacyl-synt_C; 2.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 2.
DR PROSITE; PS52004; KS3_2; 2.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000192468};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SMC21807.1}.
FT DOMAIN 603..680
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 701..1157
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 2117..2194
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2218..2678
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
SQ SEQUENCE 3064 AA; 342578 MW; BAA36C73F9325760 CRC64;
MKNSFSTDKP KLSILKGKPI KELYYKKGNL GNLLIEAASS EEDNGITFVD EFYNESYLSY
KQILEKAYLA LGSLQENGVK KGSYVMLIIE ENIDFVINFW ACVLGGAIPI PLTHPSALTK
GNSSVDKILN ICESLEKPII IVDENKKEAY VSLVKSEQMD TVKLLGTNDT RVSKVNGILS
LADVNSPAFI QFSSGSTNTP KGVILTHENI LVNIESMVNR LKINSEDTIM NWMPFSHDMG
LIGFHILEVA TVSKIVNIST TTFVKNPGIW LDLVTKYKAT VTSSPNFGYK ILLQRLNEKQ
LANWKLNSLR VIINGAEPIS EVLVNTFFHK LSSCGLKSSS MNLSYGMAEA ALAISISPLN
SNPIFHYSDR NKMSKESKIE ISMNKKEKTI AVADLGQILD GMELRIVDET GKVITENNIG
EIQIKGRNVT SGYLNNEELN KEIFENGWFK TGDMGFVRDG RLSITGRIKD IIFINGQNFY
SHDIEDRIEG IDGIEPGKIA VCGYHDEVEN KEKVVLFSNL SVDAKVYSQI ISFVSESIGF
NLDYIVIVNN IPKTNSGKVQ RFQLMKAFKA KQFVDSTYTA SKYLLLDETK AVCKNRSKIK
TGINTDSYLE TIRDIWAKVL ELPKENINCE KSFLSLGGNS IRAIQMLSYI EDELNIKLSH
DILIECHTIN EMNDYLLKRP NYIMPNNSNG SSDKNINRSE SEDIAVISMA GYFPGAKNLE
EFWNDLKKGK SNFTKIPNSR FDIENYYNKD KQSGKTYCDV GGFIDNPYAF DPKFFNISEE
EANVMDPQQR IILELVFKVL EEGGYSKAAV DGKNIGMFIG AGTNNYLEYH LNTLKINDIK
EFSSFEELSQ NQKKQFVEEW NSKFGYTENH PNLLVDNIIN MIAARASHEF NFKGPSLTVD
TACSSALVTI HLACESLRNK ECEMAIAGGV NLLLTPTPYV LFSNAGALSL SGKSKIFDEE
ADGFVPGEGA GTVLLKPLSK AIDDKDDILA IIKGSAISND GRSIGVMAPN PDGQRSVIES
LYAKKGISPK EIQYVEAHGT GTKIGDPSEV RALSEAYSKW NTEDKSIAIG SVKANVGHLL
NAAGIASFIK VVLALKNRTL PPSINVTKPN PLIKFDKTPF YLVNKAKEWT IGKEEKRRAA
VNSFGFGGTN CHMILEEAPE IVNYKEIKTN TLPKNILCLG ANNNVALKQK VTNLYEFLKV
NGNYFLGDVC YTENLRSMDF KTKCSIVADD INDLIKKLEG LKLKNNEVIN FKKIAFMFTG
QGSQYVGMAK DIYEVIPEFR AHLDECSEVF YPYIKAKITD LIYSENAENN VLKNTNITQP
VVFAIDYSFG KMLMDYGIKP DCVLGHSIGE WAAACIAEVI SLKEAARLVS LRGKLMNEIK
IQGAMAAVFL SKDKLAELFD KIKPDELWIA AYNGSHQVIS GKSQSVDKFI NILERQGIVC
KKLKVSEAFH TPLMKSMLAE FEKEMENIKF KEPKIKIVSN ITGTFIETPM KLEYWLKHIL
SSVRFEQSVK FIYDQGITNF IECGPDKILS GMAKAVLINN DVNIMPLLDR KKDNLDVFLG
TIGDLNSLGF KFDWAKFFMN FKYNKVKLPL YPFEKSTYGP QFGTLIKKSI APKEWFYSWK
WKEDVKIGEK EIGEGAIIVF ADELSIGQQL EYNFDNKTNP VYFVKTGKNF IYDGKNNFVI
DPDNRRDYKN VLNEIPNKIS TIIHLWTLNH GEFNPKLEIL NHKLINENFY SILFMADAIK
SKAEESIDFV VVTNRAQKVK QDENISSPYA SLATTLTQAI GEDNTEIRCK IIDIDVNAYK
TNSDISSTLF NELTIMPNEE NIIAIRDNKG FERKLEQLDV IEKSLEIKDG ETYLITGGVG
PLCGDIALSL AKKAKINLVL TGRSVLPERE LWNQTTSDIS LKEKISLLME LEKLGAKVMY
FSVDVADYDT MKKCIEEVKN KFGHIDGVLH GAGVVDYSEF NLFKKDLNTV NKVLAPKVQG
TIITDMLTRN EPLKFFVMLS SVSASKKKWS SGIGDYAAAN AFLSSYSIYR NQANAKGKTV
AINYSLWEEK GMGKTFGKGA EQAAKVQGLR PLKAEKAVNA FFKAVAFHKI NNVHVIDYIS
EEKAKNTEVK EKVLSYMEIE ENKNTIYKII ADELKVSKDN LETETNFMEL GLDSVGAMKI
MANLSAAFKK ELYPTLIFEY QTPVALANYI EKNYFTTKKE TYVEEEEKDL NEVDKEKTSD
IAIIGISLRI PGANNLDEYW KILNDGKVVI KDVPEERWSI RDEYSTEKDS LHTTYSKCGG
FIDRAYGFDP LFFGISPKEA EVMDPQQRVF LEVAFEALQE AGYIGKYKTQ KIGVFVGSEQ
NSYMEHFTNY RNYKMLKSSF ENSPWFKNME MDEKRSVLKA LINVLKPKEL MADSVAGNGL
NEIAARVSHC LNLMGPSLVV NTACSSSLVA LHLACENLKA NQSEIAIVGG VNLNLSSIPF
ISMSKLNAIS PNGECRPFDG DANGMVLSEG VSAIVIKPMK KAMEDGDNIY AVIKGSAINN
DGHSQGITAP NPNGQAIAVE MAYKNSGVNP ETVSYIEAHG TGTPLGDPIE IQGMTKAFRS
FTDKNQFCAI SSVKASIGHM LAASGLVSLI KVVLAMKHNT IPKTVNFKNV NPNINFESTP
FFVAKENIKW KAKDENPLRA GVNAFGFGGT NAHIVIEESP IIKAEKNDDK IGTHLLQITG
KNQNTIKKIS ENLINYVEQN PEIEISAICD TMNSSQKQLI YKTSVVAESK RDLLDKLYAI
SEGVMTDEMY NGKINPNKET RCHLLLDGNF KADKNDIQVL KNRFKVFKTA YNTCSSYYES
IQVGKTSSEE IDEKVEMFSL EYSFGALLES LQIKFTTIIS KGFGILSGAA LTGKITINQG
INIILDENID INEKKRAKIN SPLITVQGAI DCSDEEDLLY ILDLVYDNEL FPNLNEIVKE
KETILYLGTS KEIEAELEGL SIGAKLINEN LTSSLEKSFL SALGKMYTLN ISYNPKNLYS
NYKIIKTALP TYPFDNVDYK MSLENNDYMD YSLQKIDNII RLSPNDKKNS FAKLSDDFKL
NKGL
//
