PKSM_BACSU
ID PKSM_BACSU Reviewed; 4262 AA.
AC P40872; O31781;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Polyketide synthase PksM;
GN Name=pksM; Synonyms=pksY; OrderedLocusNames=BSU17200;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [2]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-1763.
RC STRAIN=168 / PB1424;
RA Tognoni A., Grandi G.;
RL Submitted (JUL-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBCELLULAR LOCATION.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17190806; DOI=10.1073/pnas.0609073103;
RA Straight P.D., Fischbach M.A., Walsh C.T., Rudner D.Z., Kolter R.;
RT "A singular enzymatic megacomplex from Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:305-310(2007).
RN [6]
RP FUNCTION IN BACILLAENE BIOSYNTHESIS.
RC STRAIN=168 / Marburg / ATCC 6051 / DSM 10 / JCM 1465 / NBRC 13719 / NCIMB
RC 3610 / NRRL NRS-744 / VKM B-501;
RX PubMed=17234808; DOI=10.1073/pnas.0610503104;
RA Butcher R.A., Schroeder F.C., Fischbach M.A., Straight P.D., Kolter R.,
RA Walsh C.T., Clardy J.;
RT "The identification of bacillaene, the product of the PksX megacomplex in
RT Bacillus subtilis.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1506-1509(2007).
CC -!- FUNCTION: Involved in some intermediate steps for the synthesis of the
CC antibiotic polyketide bacillaene which is involved in secondary
CC metabolism. {ECO:0000269|PubMed:17234808}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 4 phosphopantetheines covalently. {ECO:0000305};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17190806}.
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DR EMBL; AL009126; CAB13603.3; -; Genomic_DNA.
DR EMBL; Z35133; CAA84505.1; -; Genomic_DNA.
DR PIR; C69679; C69679.
DR RefSeq; NP_389601.3; NC_000964.3.
DR RefSeq; WP_003245093.1; NZ_JNCM01000035.1.
DR SMR; P40872; -.
DR STRING; 224308.BSU17200; -.
DR PaxDb; P40872; -.
DR PRIDE; P40872; -.
DR EnsemblBacteria; CAB13603; CAB13603; BSU_17200.
DR GeneID; 940026; -.
DR KEGG; bsu:BSU17200; -.
DR PATRIC; fig|224308.179.peg.1865; -.
DR eggNOG; COG0236; Bacteria.
DR eggNOG; COG0451; Bacteria.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR InParanoid; P40872; -.
DR OMA; MHKDYSL; -.
DR BioCyc; BSUB:BSU17200-MON; -.
DR UniPathway; UPA01003; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0004312; F:fatty acid synthase activity; IBA:GO_Central.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0071770; P:DIM/DIP cell wall layer assembly; IBA:GO_Central.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IBA:GO_Central.
DR Gene3D; 1.10.1200.10; -; 4.
DR Gene3D; 3.10.129.110; -; 2.
DR Gene3D; 3.40.47.10; -; 3.
DR Gene3D; 3.40.50.150; -; 1.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020807; PKS_dehydratase.
DR InterPro; IPR042104; PKS_dehydratase_sf.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR020615; Thiolase_acyl_enz_int_AS.
DR Pfam; PF16197; KAsynt_C_assoc; 2.
DR Pfam; PF00109; ketoacyl-synt; 3.
DR Pfam; PF02801; Ketoacyl-synt_C; 3.
DR Pfam; PF08659; KR; 2.
DR Pfam; PF08242; Methyltransf_12; 1.
DR Pfam; PF00550; PP-binding; 4.
DR Pfam; PF14765; PS-DH; 2.
DR SMART; SM00826; PKS_DH; 1.
DR SMART; SM00825; PKS_KS; 3.
DR SMART; SM00823; PKS_PP; 4.
DR SUPFAM; SSF47336; SSF47336; 4.
DR SUPFAM; SSF51735; SSF51735; 3.
DR SUPFAM; SSF53335; SSF53335; 1.
DR SUPFAM; SSF53901; SSF53901; 3.
DR PROSITE; PS00606; B_KETOACYL_SYNTHASE; 2.
DR PROSITE; PS50075; CARRIER; 4.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
DR PROSITE; PS00098; THIOLASE_1; 1.
PE 1: Evidence at protein level;
KW Acyltransferase; Antibiotic biosynthesis; Coiled coil; Cytoplasm;
KW Multifunctional enzyme; NADP; Phosphopantetheine; Phosphoprotein;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..4262
FT /note="Polyketide synthase PksM"
FT /id="PRO_0000180300"
FT DOMAIN 293..367
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2188..2261
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3409..3486
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 4135..4212
FT /note="Carrier 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 396..834
FT /note="Beta-ketoacyl synthase 1"
FT REGION 2275..2313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2322..2737
FT /note="Beta-ketoacyl synthase 2"
FT REGION 3532..3947
FT /note="Beta-ketoacyl synthase 3"
FT COILED 2750..2826
FT /evidence="ECO:0000255"
FT COILED 4004..4033
FT /evidence="ECO:0000255"
FT COMPBIAS 2275..2292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2293..2307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 569
FT /note="For beta-ketoacyl synthase 1 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 2476
FT /note="For beta-ketoacyl synthase 2 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT ACT_SITE 3690
FT /note="For beta-ketoacyl synthase 3 activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10022"
FT MOD_RES 327
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2222
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3446
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 4172
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 78
FT /note="K -> E (in Ref. 4; CAA84505)"
FT /evidence="ECO:0000305"
FT CONFLICT 703..715
FT /note="AHGTGTSLGDPIE -> PMALAPHWEIRLK (in Ref. 4;
FT CAA84505)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 4262 AA; 475621 MW; 7EC71F5C6358145F CRC64;
MITEQLHISL NNPIMSNHKV YGQALLPGLA YIDLIYQVFQ EHGYAYQELE LKNLTIFYPL
IADESYDIAL TIHVSERKEG TWSIIIDGQK QHGESLSDKR QYVTADMHRK EQTAFAESID
LNQWKSTADR ILNLDEIYEQ CRSQELVHTG MMKAEGQIYE AKEGAVIDLA VGQEALRHSD
AFLFHPTLID GSGIGSSCLI SDQTMYLPLY YESFSASERL QKGCTARILS SSVRQKKELT
YMTIEYFNSA GQKVAELKQF AGKSVRNMSA FHSAKEIQEE RAAVSQNISR DYPAFEMYLR
QLLAKQLERP AEQMDIHAGY YELGLDSSSL LTVVQEIGDK VGADLAPTLL FEFTTIAELA
AHLADHYSIG EADDAVRQSP SPIDGVTSSP EIGEDIAIIG MAGRYPKAKN IQEFWEQLKA
GTDCITEIPN SRWEWKESDG LDSPAGKPLS KWGGFIEEAD CFDPQFFRIS PREAEMMDPQ
ERLFLETCWE AIEDAGYTPE TIASPQGENK RQHVGVFAGV MHKDYSLIGA EALSEHNPFP
LSLNYAQIAN RVSYYCNFHG PSMAVDTVCS SSLTAVHLAI ESIRNGECEA ALAGGVNLSL
HPAKYISYGS VGMHSSDGYC HTFGKGGDGY VSGEGVGTVL LKPLRKAEQD GDRIYAVIKG
SAINHVGKVS GITVPSPVAQ ADVIEACLEK TGIDPRTISY VEAHGTGTSL GDPIEVQGLV
KAFSRNTQDK QFCSIGSVKS NIGHAEAAAG ISGLTKTVLQ LHHKTLVPSL HSEELNPYLK
LDQTPFFVQH ETKEWEQPSF TENGVDVTYP RRAGLSSFGA SGSNAHLILE EYIPAESHSE
TILTKNEEIV IPLSARNKDR LQAYALKLLD FLSEDVNLLA LAYTMQAGRV EMEERAAFIV
KDIKDLTAKL RAFANGEEEI EGCWTGRAKE NQEAAGLASV NALNNNLIRD SEMMEMAKAW
VQGKRVTWDD LYGDRKPLKI SVPTYPFARE RYWISVPEMK TSTVNHILHP LVHRNTSDFT
EQRFSSVFTG TEFFLSDHVV QGQKILPGVA YLEMAREAAE KAAGDLDGEQ RVVSLKDIVW
VRPITIESEP KEIHIGLFPE DNGDISFDIY SSSEHKEEAL TIHCQGRAVI SDEAETSILN
LSSIQTECSL DTVTSEQCYA AFRKIGLDYG EGYQGIEKVY VGKDQLLAKI SLPAFLKNDK
QHFALHPSLM DSAFHATVGF IVSSVNAAGQ AQTLSLPFAL QEVDIFSPCP EKIWSYIRYS
SDSKAENKVR KYDIDLCDEN GRVCVRMKGA SMRALDGEQH SKPQLLTDSQ LTGHTVMIPV
WEPVSLEAED NASFAGKRAV LCGAAEADRT FIKHHYPQIS FVDIRPADDI EAIADKLQAY
GSIDHVLWIA PSHRGSIGSD GQEEAVLHLF KLVKACLQLG YGEKQLEWSL VTVQAQPVTQ
HEAVQPAHAS IHGLAGTMAK EYPHWKIRLL DLEKGCTWPV NHMFALPADR LGHAWAYRNQ
QWHQQQLIPY RSSLSGDTLY RKGGVYVVIG GAGYIGEAWS EYMIRRYQAQ IVWIGRSQLN
AAIQSKIDRL SALGPEPFYI AADAADKHSL QQAYEQVKKR HPHIHGIVHS AMVLFEQSLE
KMKPEEFTAG LAAKIDVSIR MAQVFRQENV DFVLFFSSLV AHIKNVKQSH YASGCTFADA
FAHQLSQSWA CPVKVMNWGY WGNSEAAEDE HYVQLMNQIG LGLIEPAEAM KALEALLSGP
VSQTAFIHTT KPVAVEGVNQ NEFITLYPEQ PSADAESLME RLPTTGRFQR VTHEELDDLL
YRLLLGQLQT AELFDGYTLS VERLQQYKTR EFYGKWIRQS SEFLLQHGYL KKVGDSLVRK
DQAEDIELLW LEWNAKKEKW LKDSETKAMV VLAEAMLQAL PDILTGKVPA TDIMFPHSSM
ELVEGIYKHN QVADYFNKVL ADTLLAYLDE RLKHDPEASI RIMEIGAGTG GTSAGIFEKL
KPYQKHINEY CYTDLSKAFL LHAEKEYGAE NPYLTYQLFD VEKPIDQQEF EAGGYDVVIA
ANVLHATKNI RQTLRHTKAV MKNNGMLLLN EMAGNSLFPH ITFGLLEGWW LYEDPAVRIP
GCPGLHPDSW KAALESEGFE SVFFPAEAAH DLSHQIVAAS SNGLVRRMMK NVILPEKVVS
QASNQEPAYI HTIDSEEAGQ SKHALLREKS TEYMKKLIGE TLKIPAGKIE SSEPLEKYGI
DSIVVVQLTN TLRKEFDHVS STLFFEYQTI DALVEHFIKT KTEALMKLTG LDRQVQQHTP
AESRTQSSQK PDQAAKRTRR FRKLGFSGEK ETPTNTLASR DVAVIGISGR YPQAETAEDF
WNNLKEGRNC IEEIPKDRWD WKAYYDKEKG KEGSIYTKWG GFIKDMDKFD PLFFQISPLE
AERMDPQERL FLQTAYASIE DAGYTPDSLC SSRKIGVFAG VMNKNYPTGY GYWSIANRIS
YLLNFQGPSL AVDTACSSSL TAIHLALESI YSGSSDCAIA GGVNLVVDPV HYQNLSVMNM
LSASDTCKSF GDDADGFVDG EGVGAIVLKP LQQAIADGDH IYGVIKASAI NSGGKTNGYT
VPNPHAQAQV IKEAIERADI PARTISYLEA HGTGTALGDP IEIAGLTKAF EKDTQEKQFC
AIGSSKSNIG HCESAAGIAG LTKILFQFKY GQIAPSLHAQ RLNPNIEFSH TPFVVQQQLG
EWKRPVIGGQ EVPRRAGLSS FGAGGSNAHI ILEEYIPRTG AQTPKDHPPA LIVLSAKNME
RLQEKAEQLL TAIKQKRYCE TDLIRIAYTL QTGREAMEER LAFIAESLED LERKLNDFIE
NKADSLYLDR IDDNKKALAV LSADEDTEKI IEAWMSKGKY TKLLDLWVKG LSFDWGMLYG
TQTPVRISLP AYPFAKERYW APGAAKAPVS IEQDHDQQTE EPFKVMTFQE VWKEEPATLT
SKRIKTLICF LTEREKQNAF ASALKNVDQD TKVIFISQGE VYSKQSEYSY QIVRQEPVTF
EKAFQSIKEE LGEPDAILYM WPMEDKRCIK DHSCIVYLLQ GMSAAKLHPS RLLLAGCFED
SLDRSYLESW IGFERSLGLV LPHTKVTGIF QPAEQGSMDD WTRKVWAELQ ASTEQTVLYQ
NLKRYVNHIE QTTIQPDNSK LKSGGTYLIT GGVGGLGYLF AKHLAKNYAA NLILTGRSPF
NDEKQKQIKE LKDLGGEAMY AEADVSDPIA MGDCVKRGKD RFGAINGVIH AAGIESDSAI
FDKKIESFQR IIEPKINGTI ALDEWLKNED LDFMCYFSSS SAVLGDFGCC DYAIGNRFQM
AYAQYRNELH NGKTFVINWP VWKDGGMKIG DEETTDMYLK SSGQRFLEAE EGIRMFEHIL
AQQDAQHLVI AGQPSRVSRF LGMTEPAIPE PATQAPLAQE NKDEVKTLSI EKRLEHDLKE
HIHTLLKISK DKLNLNKNWA DFGFDSIYLA KFSNVLSKHF NIEVTPALFF GYSTLQELIS
FFLTDHKELI EAFYRDDASE AQKPPEAYAV IPVALEPEAS KKSIRQVHDE PIAIIGMSGR
FPQADSVHEL WDNLKNGKSC ISDIPGERRD WGRANRDPEK AVPRWGAFLK DIDRFDPLFF
QISPKEAESM DPRQRIFLEE AWHTFEDAGY MGDRIKGKSC GVYVGVEEGE YAHLTGDTDY
INGTQNATLS ARIAYALDLK GPNMALTAAC SSGLVAIHQA CSALRQGDCE MALAGGVSLN
ISHMSFEALT RAEMLSPNGQ CKVFDQDANG LVPGEAVAAV LLKPLSKAIE DKDHIYGCIK
ASGVNYDGKT NGITAPNPFS QAELIENIYE KNEINPLDIQ YVMAHSTGSN LGDPLEVQAL
TSVFSKYTKQ KQFCMISSIK PLIGHTFAAS GTVALISMLM AMKNQIIPAT HHCESENPYI
PFKESPFVLC KENRSWIKKN QKPRMGTIST TGISGTNAHA VIEEYIPDDQ PSTQRHQGSP
QIFVISAQND DRLQDAACRM IAYLEQNHNL SLPDVAYTLQ VGRKAMEARL AIVANNQEQL
VRKLKEYVEA MKNGGVSGQQ RSLYTGYTEG ILEEQDEAVL QALAKERNLE NIAECWVKGY
QIPWELLHDG DDVRMVSLPG YPFARERYWI SSGTQQSEAV KQHSQDMKTE IDEPNGKTHI
QKIIVQFLAR ELGISEDRIN FKRNFLDYGM DSILGRKLMR HIEKTTQLKM AGREILECQT
VQALSDHLAL KAEKQNHSAA AHHIKGTYTD EQIIGLMQEV ALGKLDFKSV QNIIEGSKSY
ES
