PPSD_BACSU
ID PPSD_BACSU Reviewed; 3603 AA.
AC P94459; Q796G3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Plipastatin synthase subunit D;
DE EC=2.3.1.-;
DE AltName: Full=Peptide synthase 4;
DE Includes:
DE RecName: Full=ATP-dependent proline adenylase;
DE Short=ProA 1;
DE AltName: Full=Proline activase 1;
DE Includes:
DE RecName: Full=ATP-dependent glutamine adenylase;
DE Short=GlnA;
DE AltName: Full=Glutamine activase;
DE Includes:
DE RecName: Full=ATP-dependent tyrosine adenylase 2;
DE Short=TyrA 2;
DE AltName: Full=Tyrosine activase 2;
GN Name=ppsD; Synonyms=pps4; OrderedLocusNames=BSU18310;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7711903; DOI=10.1099/13500872-141-3-645;
RA Tognoni A., Franchi E., Magistrelli C., Colombo E., Cosmina P., Grandi G.;
RT "A putative new peptide synthase operon in Bacillus subtilis: partial
RT characterization.";
RL Microbiology 141:645-648(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA de Ferra F., Tognoni A.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
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 [4]
RP SEQUENCE REVISION TO 46; 1293; 1303; 1324; 1530; 1533 AND 1743.
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 [5]
RP FUNCTION IN PLIPASTATIN BIOSYNTHESIS.
RX PubMed=10471562; DOI=10.1128/aac.43.9.2183;
RA Tsuge K., Ano T., Hirai M., Nakamura Y., Shoda M.;
RT "The genes degQ, pps, and lpa-8 (sfp) are responsible for conversion of
RT Bacillus subtilis 168 to plipastatin production.";
RL Antimicrob. Agents Chemother. 43:2183-2192(1999).
CC -!- FUNCTION: This protein is a multifunctional enzyme, able to activate
CC and polymerize the amino acids Pro, Gln and Tyr as part of the
CC biosynthesis of the lipopeptide antibiotic plipastatin. The Tyr residue
CC is further epimerized to the D-isomer form. The activation sites for
CC these amino acids consist of individual domains.
CC {ECO:0000269|PubMed:10471562}.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 3 phosphopantetheines covalently. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; Z34883; CAA84363.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13714.2; -; Genomic_DNA.
DR PIR; D69681; D69681.
DR RefSeq; NP_389713.2; NC_000964.3.
DR RefSeq; WP_009967354.1; NZ_CP053102.1.
DR SMR; P94459; -.
DR STRING; 224308.BSU18310; -.
DR PaxDb; P94459; -.
DR PRIDE; P94459; -.
DR EnsemblBacteria; CAB13714; CAB13714; BSU_18310.
DR GeneID; 940013; -.
DR KEGG; bsu:BSU18310; -.
DR PATRIC; fig|224308.43.peg.1941; -.
DR eggNOG; COG1020; Bacteria.
DR InParanoid; P94459; -.
DR OMA; CQFEYST; -.
DR PhylomeDB; P94459; -.
DR BioCyc; BSUB:BSU18310-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 3.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.30.559.10; -; 4.
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.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR010060; NRPS_synth.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 3.
DR Pfam; PF13193; AMP-binding_C; 3.
DR Pfam; PF00668; Condensation; 4.
DR Pfam; PF00550; PP-binding; 3.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 3.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 3.
DR TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR PROSITE; PS00455; AMP_BINDING; 3.
DR PROSITE; PS50075; CARRIER; 3.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 1: Evidence at protein level;
KW Antibiotic biosynthesis; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Reference proteome; Repeat; Transferase.
FT CHAIN 1..3603
FT /note="Plipastatin synthase subunit D"
FT /id="PRO_0000360844"
FT DOMAIN 966..1041
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1997..2072
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 3034..3108
FT /note="Carrier 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 7..1043
FT /note="Domain 1 (proline-activating)"
FT REGION 7..306
FT /note="Condensation 1"
FT REGION 490..889
FT /note="Adenylation 1"
FT REGION 1053..2069
FT /note="Domain 2 (glutamine-activating)"
FT REGION 1053..1334
FT /note="Condensation 2"
FT REGION 1521..1924
FT /note="Adenylation 2"
FT REGION 2084..3596
FT /note="Domain 3 (proline-activating)"
FT REGION 2084..2374
FT /note="Condensation 3"
FT REGION 2560..2956
FT /note="Adenylation 3"
FT REGION 3116..3596
FT /note="Epimerization"
FT MOD_RES 1001
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2032
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 3069
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT CONFLICT 46
FT /note="N -> T (in Ref. 1; CAA84363)"
FT /evidence="ECO:0000305"
FT CONFLICT 1293
FT /note="L -> W (in Ref. 1; CAA84363)"
FT /evidence="ECO:0000305"
FT CONFLICT 1303
FT /note="V -> A (in Ref. 1; CAA84363)"
FT /evidence="ECO:0000305"
FT CONFLICT 1324
FT /note="V -> A (in Ref. 1; CAA84363)"
FT /evidence="ECO:0000305"
FT CONFLICT 1530
FT /note="N -> T (in Ref. 1; CAA84363)"
FT /evidence="ECO:0000305"
FT CONFLICT 1533
FT /note="A -> S (in Ref. 1; CAA84363)"
FT /evidence="ECO:0000305"
FT CONFLICT 1743
FT /note="H -> Q (in Ref. 1; CAA84363)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3603 AA; 406812 MW; 9A30389D45FEC274 CRC64;
MTKANSIQDI YPLSYMQEGM LFHSLLQKDS QAYVEQASFT IEGKVNPQFF QNSINALVER
HDIFRTIFIS QNVSSPQQVV LRERNVIVLE EDITHLNEAE QSQFIEQWKE KDRDRGFHLQ
KDVLMRIALI QTGESQYSCI WTFHHIMMDG WCLSIVLKEF LHIYASYVNA SPITLEPVQP
YGKYIKWLME QDKEQAVSYW DHYLSGHEQQ TVLPKQKKTK GKSRQEHVTF SFSKEESSRL
SELAAREEVT LSTIFHTIWG ILLQKYNNND DAVFGSVISG RPAEIEGIEH MVGLFINTMP
VRVQGAKTPF LQLIKDMQKD RLAAEAYSYH PLYEIQSRSA VKQGLIDHIL VFENYPVQQE
IQMLNKQEHA SDLFQIHNFT VADETNYSFY LMVAPGEEIH IKMNYDAEQH DRSFVLSVKE
HLLNAVSQIL NNPNLPPEEI DITTDTEKRQ LIGEITDQTP VYETIHAMFE KQAEKTPDAH
AVIDQACSLT YRELNKAANR LARHLRMKGV VRQEPVAIMM ERSAAFITGV LGILKAGGAI
VPVDPHYPAD RIRYILHDCG CSHVVSQAHL PSSLEDNYII THPEDIESKV DGSNIKSVNN
ADDLLYMIYT SGTTGKPKGV QFEHRNMANL LKFEYTHSGI DFEADVLQFA TPSFDVCYQE
IFSALLKGGT LHIVPEAIKR DVPQLFAFIN KHQTNIVFLP TAFIKMIFSE RELANSFPDG
VKHLIAAGEQ LMISDLFQDV LRKRGIHLHN HYGPSETHVV STYTIHPGDP IPELPPIGKP
IGCTDLYILN HQKQLQPCGV PGELYISGAS VARGYVNHDK LTSDKFSSDP FKPDVIMYRT
GDLARRLEDG NIEYIGRADN QVKIRGYRIE PQEIEVTLMN HPDISEAAIL IWQDQNGEHE
LCAYYCSVQK LNTIDLRSYM ASELPEYMIP AKWIWVDSIP LTPNGKVDRA ALPEPDASIS
GNPYTAPRNL LEAKLSQLFE DVLKNGHIGI QDNFFDNGGH SLKATVLMSR IAKEFHVQVS
LKDIFAHPTV EGLALIIREA EQNLYAAIEP AEKRDTYPVS SAQKRIYVLQ QLDEGVAYNM
PAVLELEGAL DVAKLSAVCK ELISRHEPLR TSFVSGADDE PVQRIHTEVP FTLSKETTIE
GFVRPFDLSQ APLFRAGLIE VSNEKHVLLV DMHHIISDGV SVQLLIREFT DLYANRQLKP
LRIQYKDYAV WQQKFKKGDS YQKQETYWQQ QFSGDLPILE LPTDKRRPAE RQFIGGKVTF
QLDKEITARI KRLAHKNRST LYMTLLALYS AFLSRLSGQD DIVIGSPIAG RPHADLEAVL
GMFVNTLALR TRPAGNKTFE EFLKEVRQTA LEAYEHQDYP FEELVDKLGV QREMSRNPLF
DTTLVLQNME QQKLKMNDVQ LQWNDLEHPI SKFDISLYVT EHDSELFCQF EYSTALFEKE
TIQRWASLFT TLVEHTAASP ETELDNIPIL TKEEERDFIE SCHLFEETGY SMNQTLHYAL
EQQAEKTPDQ AAVIFEDGVM TYKELNEQAN RIAWELIGRG VKPETTVAII GKRSPEMLLG
IYGILKAGGA YLPIDPDYPE ERISFLLEDS GTNILLLQSA GLHVPEFTGE IVYLNQTNSG
LAHRLSNPNV DVLPQSLAYV IYTSGSTGMP KGVEIEHRSA VNFLNSLQSR YQLKHSDMIM
HKTSYSFDAS IWELFWWPYA GASVYLLPQG GEKEPEVIAK AIEEQKITAM HFVPSMLHAF
LEHIKYRSVP IKTNRLKRVF SGGEQLGTHL VSRFYELLPN VSITNSYGPT EATVEAAFFD
CPPHEKLERI PIGKPVHHVR LYLLNQNQRM LPVGCIGELY IAGAGVARGY LNRPALTEER
FLEDPFYPGE RMYKTGDVAR WLPDGNVEFL GRTDDQVKIR GYRIEPGEIE AALRSIEGVR
EAAVTVRTDS GEPELCAYVE GLQRNEVRAQ LERLLPGYMV PAYMIEMEQW PVTPSGKLDR
NALPAPGGAA DAETYTAPRN VTEMKLSQLW EDVLKNGPVG IHDNFFDRGG HSLKATALVS
RITKEFDVQV PLKDVFAHPT VEGLATVIRE GTDSPYEAIK PAEKQETYPV SSAQKRIYVL
QQLEDGGTGY NMPAVLELEG KLNPERMDRA FQELIKRHES LRTSFEQDEG GDPVQRIHDE
VPFTLQTTVL GARTEQEAAA AFIKPFDLSQ APLFRAQIVK VSDERHLLLV DMHHIISDGV
SVNILIQEFG ELYNNRKLPA LRIQYKDYAV WQEGFKTGDA YKMQEAYWLK QLEGELPVLD
LPADHARPPV RSFAGDKVSF TLEPEVASGL HKLARENGST LYMVLLAAYT AFLSRLSGQE
DIIVGSPIAG RPHKDLEPIL GMFVNTLALR TRPEGGKPFV QYLQEVRETA LEAFEHQNYP
FEELVDKLEL TRDMSRNPVF DAMLVVQNND YEPLHLHDLQ MKPAQVSHLV SKFDLTLQAS
EGDGNIHFLF EYSTALFEKT TIERWASHLT NVLSIIGKNP KVTLNHIDIL TQEERHQLLN
EFNTGQANQY GVQTISQLFE QQAARTPKAS ALVSGDKTLT YQELDEWSNG IARALRSRGV
KPDTPVGIMM HRSFSMIASI LGVWKAGGCY VPIDPEYPKE RKRYILSDSG TKLLMTINEA
DLGVLADFEG EILTIESVEE DDKSPLPQMS SAHHLAYIIY TSGTTGRPKG VMVEHKGIAN
TLQWRRNAYA FNETDTILQL FSFSFDGFIT SMFTPLLSGA KAVLLHEEEA KDILAIKHQL
SRQRITHMII VPVLYRALLD VVQPEDVKTL RVVTLAGEAA DRELIARSLA ICPHTELANE
YGPTENSVAT TVMRHMEKQA YVSIGQPIDG TQVLILNSNH QLQPIGVAGE LCIAGTGLAR
GYVNLPELTE RAFTQNPFKP EARMYRTGDA ARWMADGTLE YLGRIDDQVK IRGYRVETKE
IESVIRCIKG VKDAAVVAHV TASGQTELSA YVVTKPGLST NAVRSELQNK LPVFMHPAFI
EKLDSLPLSP NGKLDRGALP KPVYNHEGER PFLPPSSKME QILADIWKEV LGAEKIGTAD
SFFELGGDSI KALQVSARLH RIGKQMAVKD LFSHPTIQEL AAYIRDSDTS SSQAAVEGDV
QWSPVQKWFL SQDIKEKHHF NQSVMLHRST SVQEDALRKT LKAITCHHDA LRMVFTQNEQ
GKWDQYNRPL SHSDDALYGL QMIDLSAPDG TDGNRPYEPL IKRHVLDIQQ KMDLKNGPLL
QAGLFHTIDG DFLFLSAHHL VVDGISWRVL LEDLALGYRQ AAGGEDIKLP PKTSSFKAYA
KKLSDYAESQ QLMKQLKYWR EAEEYQTEAL PFDQIDGTRA HEGQRSTISF TLNDKETAAL
LKDANSAYNT DTQDMLLASV ILALRHWTNQ SAFKLSLEGH GREDVLKGID VSRTIGWFTA
IYPLLIKLNA DLPDSEESMV HVLKTTKDTL RRVPDKGFGY GVIKYLTPPG KKDINFTGAP
EISFNYLGQF ESGRTAEVPE EDAFSFSPLG AGGDISTTWN REQSLDISAI AAEGKLTVNM
TYDNARFQRK TIEQLSETCR QFLLQLIEHC QNKSETEKTI SDFDDQELTE DALQEIADML
SFH
