UniProt: A0A0U2WJU8

Database: UniProt
Entry: A0A0U2WJU8_BACP2

LinkDB:  A0A0U2WJU8_BACP2 
Original site:  A0A0U2WJU8_BACP2

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Ontology (3)   
   GO (3)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (39)   
   InterPro (21)   
   Pfam (10)   
   PROSITE (3)   
   SMART (5)   
Literature (1)   
   PubMed (1)   
All databases (46)   

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ID   A0A0U2WJU8_BACP2        Unreviewed;      3028 AA.
AC   A0A0U2WJU8;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=Non-ribosomal peptide synthetase {ECO:0000313|EMBL:ALS35539.1};
GN   ORFNames=BPUM_03965 {ECO:0000313|EMBL:ALS35539.1};
OS   Bacillus pumilus (strain SAFR-032).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=315750 {ECO:0000313|EMBL:ALS35539.1, ECO:0000313|Proteomes:UP000001355};
RN   [1] {ECO:0000313|EMBL:ALS35539.1, ECO:0000313|Proteomes:UP000001355}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SAFR-032 {ECO:0000313|EMBL:ALS35539.1,
RC   ECO:0000313|Proteomes:UP000001355};
RX   PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA   Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA   Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA   Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA   Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA   Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA   Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA   Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA   Weinstock G.M.;
RT   "Paradoxical DNA repair and peroxide resistance gene conservation in
RT   Bacillus pumilus SAFR-032.";
RL   PLoS ONE 2:E928-E928(2007).
CC   -!- COFACTOR:
CC       Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC         Evidence={ECO:0000256|ARBA:ARBA00001957};
CC   -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC       {ECO:0000256|ARBA:ARBA00006432}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC       family. {ECO:0000256|ARBA:ARBA00029443}.
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DR   EMBL; CP000813; ALS35539.1; -; Genomic_DNA.
DR   RefSeq; WP_041815252.1; NC_009848.4.
DR   STRING; 315750.BPUM_03965; -.
DR   KEGG; bpu:BPUM_03965; -.
DR   OrthoDB; 9765680at2; -.
DR   Proteomes; UP000001355; Chromosome.
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; cd19531; LCL_NRPS-like; 1.
DR   CDD; cd00833; PKS; 1.
DR   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.30.70.3290; -; 1.
DR   Gene3D; 3.40.47.10; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR   InterPro; IPR010071; AA_adenyl_domain.
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; IPR025110; AMP-bd_C.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR049490; C883_1060-like_KR_N.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR018201; Ketoacyl_synth_AS.
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   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00698; Acyl_transf_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF21394; Beta-ketacyl_N; 1.
DR   Pfam; PF00668; Condensation; 2.
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; 2.
DR   SMART; SM00827; PKS_AT; 1.
DR   SMART; SM00822; PKS_KR; 1.
DR   SMART; SM00825; PKS_KS; 1.
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; SSF52777; CoA-dependent acyltransferases; 4.
DR   SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR   SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR   SUPFAM; SSF53901; Thiolase-like; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00606; KS3_1; 1.
DR   PROSITE; PS52004; KS3_2; 1.
PE   3: Inferred from homology;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          974..1049
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1067..1492
FT                   /note="Ketosynthase family 3 (KS3)"
FT                   /evidence="ECO:0000259|PROSITE:PS52004"
FT   DOMAIN          2492..2567
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   3028 AA;  341919 MW;  2FA84DF66BBB12AC CRC64;
     MALQPQKLDK QNIENMLGVT TIQEGLLFHH LMEPNGTAYF EQLLIEIDGP IDRDMFEQSW
     TNVTKQHEML RTLFRWQELA RPVQIVLKEH QPDIRYRDLT QAKVPLHVLK EEVTAQNREE
     RFDLQEVPFR LTLCEVNDEV SWVLISFHHI LLDGWSLGIV LSDWMSAYER LSNGDKPLLE
     QRPSYKSFVK WQQKNLQQTE AQAAYWKSVF NGWSYSELLP KSSGAYEESE SFHKYEHQVD
     TSIAESLSKF TNQYDVTLAS VMYTLWGVLL SKYANQDDIV FGTTVSGRNA DVPHIEKMTG
     LFINTLPLRV SFEQERPILE QMQEVSREIA VRNEYEHTPL SDLKKYAGMT AEQSLFDSIV
     VIENYPLDQM LTKNDQPIRI RGFEMTEQTE FDLTLSVQAF DDQLHFSLVY NPVSFSAEQI
     EKWCQHFLHL LSDACAHPHK SAAQLQLLSE EEKEKQLAVF QQYGGATSSN EPTVIDLFEA
     QVERTPAAAA VEFGDTKVTY EQLNKRVNQL AHYLQNKGVK QEQRVGILAE HSIEMVISCL
     AILKAGGAYV PIDPEYPQER IEYLLEDSGV EWLLTHPIKG LTYAYHGEKI DITQPDLYTG
     PSDNLAEAIT SEQTAYCIYT SGTTGRPKGV LIHHLGLANY IDWAKQVYVR GETRHFALYT
     SLSFDLTVTS IFTPLISGNT IMIYHHENRQ LLVEDIIKDN RVHVMKLTPS HLQFIKHLSF
     PDSQMKCFIL GGEQLETSLA KSIQQSFPQP IEIVNEYGPT ETVVGCMIHR YDQDLDQDVY
     VPIGKPAQHT DILLFDRHMN LMPEGAVGEL YIGGKGVAKG YLNRPELTEE RFVDHPFQPG
     EKIYKTGDAA RILPNGLIQF LGRNDDQVKL RGYRIETGEI EFWLNEQPEI KAAAVVVKPD
     VSGTPCLTAY VVTTAILDQA AIKQALTDQL PDYMIPTHFV QLDDMPLTAN GKLDKRALPA
     LKQAQQTKKQ AGSDHLSDTE KVIQDIWKKV LGLDEVSVHD KFFDIGGHSL NLIHVNQQLA
     KQLNQSIPMV EMFRRPTIRE LASYVSGDAE QVAADTQSVN QKIRKANEPI AIIGMAGKFP
     GAKNVEAFWR NLKNGEESIS FFSDEELLEA GIDRQTFERS DYVRAKGVID GPDLFDASFF
     GYSPGQAEMM DPQIRLLHEY AYKALEDAGY VQEDYAGKVG LFTGSTSNFQ WIQRFASSLD
     SSMSELFEVG SLNDTYTVST RIAHKLNLKG PALTLQTACS TSLVALHLAC QSIANGDSDV
     ALAGGVSILH PVKSGYVYQQ NMVKSSDGHC RAFDDQADGT VGGDGVGLVA LKALSEAIED
     GDHIYAVIKG SAINNDGDQK VGFNAPSVEG QTRVIQDALH QADVSPETIE YVETHGTGTS
     LGDPIEIEAL TKAFDTEKKQ FCRIGSVKTN IGHLDAAAGA AGLIKAVLSL EHHTFVPSLH
     FKKANENIAF EHSPFFVNTD LTDWKQPASH LRRAGVSSFG MGGTNAHVIL EEAPQRDRQQ
     MPRSAELLVL SAKSKTSLER MKEKLASQIE NTPSINLADA AYTLQTGRQP FGFRQTFVAA
     SREDALRVLR EKQGKGIGKL MHSHVEKQKI VFMFSGQGNQ YLNMGLDLYQ EEPYFKQQMD
     ACFQAYEEAT GRSLARILYP LAAEAEKARE QLASTQYAQP AIFAIEYALS MLFIEWGVRP
     DAMIGYSFGE LTAAAISGLF SLKDAMSMVA YRANAMQSSP AGVMMSVPLP EAELKPMLPK
     NISLAVVNNS SCIVSGLEEA ISEFEQELKS NRLMCMRLGG TIAAHSHVMK EAAEQFGEKL
     THMKAKSLRI PFISNLSGDW MTDTSAKDMS YWKRHMTDTV RFAEGITNIL QEDNIQLIEM
     GPGQDLSVMV NRSLNGLNQH VCHVLRHAKQ DVTDTEFLLG QMGRLWTNGL SIDWDKFHLN
     RQPWKIPLPT YAFDQTSYWY DAADRVKQEK PKQSGRKQQM DEWFYTPHWE ADLLPCVPSE
     DTSDGALLLF ADPSAFGEKV AAELLMKRNE SVVVRKGNEF TKHDEKSYTI RSHEPSDYER
     LISNLVDDKI NVSKVCHLWG LSERQPSHTE EEWVKQTQQD SYYSLLYIGQ ALKKYVDQKV
     SITVLSSLTY AVGGEPVLYP EKAVHLGPAM VISQETPNLR YRILDIDRPV ENGVQEKRLL
     RQISDELDRA YGQLLTVYRR NKRYVKKYAK GSVPEMGHAQ LAKKDGVYIL IGGLGFIGLN
     IAQTLAEQTQ GTLILTSRSG LPDRSKWQEW LTTHDDQDPT KKKIQKVMAL EETGADVLIQ
     KVDVRHKEDI LQLIHTVDTS YGQIDGVIYA AGVTGDQSFQ VMEQTDVTFS EPHFEAKMNG
     VLHLDAALGD RSLDFCFVLS SLSPILGGLG FTAYTAVNHF IDAYVYERNL RSETQWSVIS
     FDGWEFEQGK QLDLPIGDDV TETLITEKEG RMIFERLLSL DQVEQMVIST TSLHDRIHRY
     VDRLSLEEES GREHEQDGNL YSRPALSTNY AAPETELEKA LSQHWQAFFK IDEIGIDDHF
     FEMGGDSLKA ITFIGIIHRA FSVELTLPQF FQIPTIRLMA AYIDQADTAA YHAIGKAEVK
     EHYPLSSAQK RLYLMQQMDV NSTGYNEFKA GRIKGKLDIS RLEWAFQQLI KRHESLRTAF
     VLENGVPYQK IEEEVPFAVT LFDLNNGSTQ GAEEEQKQVI EQFLTAFTLS EAPLMRVGVM
     KLAEEEFVLM LDMHHIISDG LSQDILVNDF MQLYDGRTLE PLALQYKDFS EWQNDMLASE
     ALKESSDYWK NRLEGAPLLD LPTDFDRPEV RQFRGGHYTF RIEEAELNAF KQVILKEDAT
     LFMGLLSVYH ILLHKLSGQS DITVGVPVAG RKQEELQQVI GIFVNMLPLR LYPKAELTYQ
     QFLQDVKAHV VDDFGHQDYQ YEQMVQDLQL SRSVSRNLLF DAVFALQNMN QPELKVGGLT
     FSDYPYETGT SRFDLLWIAY EQEDGLSSTI EYNTELFTKE TIERIAGLLK DIMRAVSVDV
     VRIEEIELTS SFQQLDDVSL FELDDLKI
//

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