CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-005559
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Surfactin synthase subunit 1 
Protein Synonyms/Alias
  
Gene Name
 srfAA 
Gene Synonyms/Alias
 srfA; srfA1; BSU03480 
Created Date
 July 27, 2013 
Organism
 Bacillus subtilis (strain 168) 
NCBI Taxa ID
 224308 
Lysine Modification
Position
Peptide
Type
References
1234RQAAEGYKKDQAYWKacetylation[1]
Reference
 [1] The acetylproteome of Gram-positive model bacterium Bacillus subtilis.
 Kim D, Yu BJ, Kim JA, Lee YJ, Choi SG, Kang S, Pan JG.
 Proteomics. 2013 May;13(10-11):1726-36. [PMID: 23468065
Functional Description
 This protein is a multifunctional enzyme able to activate and polymerize the amino acids Leu, Glu, Asp and Val. Activation sites for these AA consist of individual domains. 
Sequence Annotation
 DOMAIN 976 1043 Acyl carrier 1.
 DOMAIN 2015 2082 Acyl carrier 2.
 DOMAIN 3043 3109 Acyl carrier 3.
 REGION ? 1047 Domain 1 (glutamate-activating).
 REGION ? 2086 Domain 2 (leucine-activating).
 REGION ? 3114 Domain 3 (D-leucine-activating).
 MOD_RES 1006 1006 O-(pantetheine 4'-phosphoryl)serine
 MOD_RES 2045 2045 O-(pantetheine 4'-phosphoryl)serine
 MOD_RES 3073 3073 O-(pantetheine 4'-phosphoryl)serine  
Keyword
 Antibiotic biosynthesis; Complete proteome; Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Reference proteome; Repeat; Sporulation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3587 AA 
Protein Sequence
MEITFYPLTD AQKRIWYTEK FYPHTSISNL AGIGKLVSAD AIDYVLVEQA IQEFIRRNDA 60
MRLRLRLDEN GEPVQYISEY RPVDIKHTDT TEDPNAIEFI SQWSREETKK PLPLYDCDLF 120
RFSLFTIKEN EVWFYANVHH VISDGISMNI LGNAIMHIYL ELASGSETKE GISHSFIDHV 180
LSEQEYAQSK RFEKDKAFWN KQFESVPELV SLKRNASAGG SLDAERFSKD VPEALHQQIL 240
SFCEANKVSV LSVFQSLLAA YLYRVSGQND VVTGTFMGNR TNAKEKQMLG MFVSTVPLRT 300
NIDGGQAFSE FVKDRMKDLM KTLRHQKYPY NLLINDLRET KSSLTKLFTV SLEYQVMQWQ 360
KEEDLAFLTE PIFSGSGLND VSIHVKDRWD TGKLTIDFDY RTDLFSREEI NMICERMITM 420
LENALTHPEH TIDELTLISD AEKEKLLARA GGKSVSYRKD MTIPELFQEK AELLSDHPAV 480
VFEDRTLSYR TLHEQSARIA NVLKQKGVGP DSPVAVLIER SERMITAIMG ILKAGGAYVP 540
IDPGFPAERI QYILEDCGAD FILTESKVAA PEADAELIDL DQAIEEGAEE SLNADVNARN 600
LAYIIYTSGT TGRPKGVMIE HRQVHHLVES LQQTIYQSGS QTLRMALLAP FHFDASVKQI 660
FASLLLGQTL YIVPKKTVTN GAALTAYYRK NSIEATDGTP AHLQMLAAAG DFEGLKLKHM 720
LIGGEGLSSV VADKLLKLFK EAGTAPRLTN VYGPTETCVD ASVHPVIPEN AVQSAYVPIG 780
KALGNNRLYI LDQKGRLQPE GVAGELYIAG DGVGRGYLHL PELTEEKFLQ DPFVPGDRMY 840
RTGDVVRWLP DGTIEYLGRE DDQVKVRGYR IELGEIEAVI QQAPDVAKAV VLARPDEQGN 900
LEVCAYVVQK PGSEFAPAGL REHAARQLPD YMVPAYFTEV TEIPLTPSGK VDRRKLFALE 960
VKAVSGTAYT APRNETEKAI AAIWQDVLNV EKAGIFDNFF ETGGHSLKAM TLLTKIHKET 1020
GIEIPLQFLF EHPTITALAE EADHRESKAF AVIEPAEKQE HYPLSLAQQR TYIVSQFEDA 1080
GVGYNMPAAA ILEGPLDIQK LERAFQGLIR RHESLRTSFV LENSTPRQKI HDSVDFNIEM 1140
IERGGRSDEA IMASFVRTFD LAKAPLFRIG LLGLEENRHM LLFDMHHLIS DGVSIGIMLE 1200
ELARIYKGEQ LPDLRLQYKD YAVWQSRQAA EGYKKDQAYW KEVFAGELPV LQLLSDYPRP 1260
PVQSFEGDRV SIKLDAGVKD RLNRLAEQNG ATLYMVMLSA YYTLLSKYTG QDDIIVGTPS 1320
AGRNHSDTEG IIGMFVNTLA IRSEVKQNET FTQLISRVRK RVLDAFSHQD YPFEWLVEDL 1380
NIPRDVSRHP LFDTMFSLQN ATEGIPAVGD LSLSVQETNF KIAKFDLTVQ ARETDEGIEI 1440
DVDYSTKLFK QSTADRLLTH FARLLEDAAA DPEKPISEYK LLSEEEAASQ IQQFNPGRTP 1500
YPKDKTIVQL FEEQAANTPD HTALQYEGES LTYRELNERA NRLARGILSL GAGEGRTAAV 1560
LCERSMDMIV SILAVLKSGS AYVPIDPEHP IQRMQHFFRD SGAKVLLTQR KLKALAEEAE 1620
FKGVIVLADE EESYHADARN LALPLDSAAM ANLTYTSGTT GTPKGNIVTH ANILRTVKET 1680
NYLSITEQDT ILGLSNYVFD AFMFDMFGSL LNGAKLVLIP KETVLDMARL SRVIERENIS 1740
ILMITTALFH LLVDLNPACL STLRKIMFGG ERASVEHVRK ALQTVGKGKL LHMYGPSEST 1800
VFATYHPVDE LEEHTLSVPI GKPVSNTEVY ILDRTGHVQP AGIAGELCVS GEGLVKGYYN 1860
RPELTEEKFV PHPFTSGERM YKTGDLARWL PNGDIEFIGR IDHQVKIRGQ RIELGEIEHQ 1920
LQTHDRVQES VVLAVDQGAG DKLLCAYYVG EGDISSQEMR EHAAKDLPAY MVPAVFIQMD 1980
ELPLTGNGKI DRRALPIPDA NVSRGVSYVA PRNGTEQKVA DIWAQVLQAE QVGAYDHFFD 2040
IGGHSLAGMK MLALVHQELG VELSLKDLFQ SPTVEGLAQV IASAEKGTAA SISPAEKQDT 2100
YPVSSPQKRM YVLQQLEDAQ TSYNMPAVLR LTGELDVERL NSVMQQLMQR HEALRTTFEI 2160
KDGETVQRIW EEAECEIAYF EAPEEETERI VSEFIKPFKI DQLPLFRIGL IKHSDTEHVL 2220
LFDMHHIISD GASVGVLIEE LSKLYDGETL EPLRIQYKDY AVWQQQFIQS ELYKKQEEHW 2280
LKELDGELPV LTLPTDYSRP AVQTFEGDRI AFSLEAGKAD ALRRLAKETD STLYMVLLAS 2340
YSAFLSKISG QDDIIVGSPV AGRSQADVSR VIGMFVNTLA LRTYPKGEKT FADYLNEVKE 2400
TALSAFDAQD YPLEDLIGNV QVQRDTSRNP LFDAVFSMQN ANIKDLTMKG IQLEPHPFER 2460
KTAKFDLTLT ADETDGGLTF VLEYNTALFK QETIERWKQY WMELLDAVTG NPNQPLSSLS 2520
LVTETEKQAL LEAWKGKALP VPTDKTVHQL FEETAQRHKD RPAVTYNGQS WTYGELNAKA 2580
NRLARILMDC GISPDDRVGV LTKPSLEMSA AVLGVLKAGA AFVPIDPDYP DQRIEYILQD 2640
SGAKLLLKQE GISVPDSYTG DVILLDGSRT ILSLPLDEND EENPETAVTA ENLAYMIYTS 2700
GTTGQPKGVM VEHHALVNLC FWHHDAFSMT AEDRSAKYAG FGFDASIWEM FPTWTIGAEL 2760
HVIEEAIRLD IVRLNDYFET NGVTITFLPT QLAEQFMELE NTSLRVLLTG GDKLKRAVKK 2820
PYTLVNNYGP TENTVVATSA EIHPEEGSLS IGRAIANTRV YILGEGNQVQ PEGVAGELCV 2880
AGRGLARGYL NREDETAKRF VADPFVPGER MYRTGDLVKW TGGGIEYIGR IDQQVKVRGY 2940
RIELSEIEVQ LAQLSEVQDA AVTAVKDKGG NTAIAAYVTP ESADIEALKS ALKETLPDYM 3000
IPAFWVTLNE LPVTANGKVD RKALPEPDIE AGSGEYKAPT TDMEELLAGI WQDVLGMSEV 3060
GVTDNFFSLG GDSIKGIQMA SRLNQHGWKL EMKDLFQHPT IEELTQYVER AEGKQADQGP 3120
VEGEVILTPI QRWFFEKNFT NKHHWNQSVM LHAKKGFDPE RVEKTLQALI EHHDALRMVY 3180
REGQEDVIQY NRGLEAASAQ LEVIQIEGQA ADYEDRIERE AERLQSSIDL QEGGLLKAGL 3240
FQAEDGDHLL LAIHHLVVDG VSWRILLEDF AAVYTQLEQG NEPVLPQKTH SFAEYAERLQ 3300
DFANSKAFLK EKEYWRQLEE QAVAAKLPKD RESGDQRMKH TKTIEFSLTA EETEQLTTKV 3360
HEAYHTEMND ILLTAFGLAM KEWTGQDRVS VHLEGHGREE IIEDLTISRT VGWFTSMYPM 3420
VLDMKHADDL GYQLKQMKED IRHVPNKGVG YGILRYLTAP EHKEDVAFSI QPDVSFNYLG 3480
QFDEMSDAGL FTRSELPSGQ SLSPETEKPN ALDVVGYIEN GKLTMSLAYH SLEFHEKTVQ 3540
TFSDSFKAHL LRIIEHCLSQ DGTELTPSDL GDDDLTLDEL DKLMEIF 3587 
Gene Ontology
 GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
 GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
 GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
 GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW. 
Interpro
 IPR010071; AA_adenyl_domain.
 IPR009081; Acyl_carrier_prot-like.
 IPR020845; AMP-binding_CS.
 IPR000873; AMP-dep_Synth/Lig.
 IPR001242; Condensatn.
 IPR010060; NRPS_synth.
 IPR020806; PKS_PP-bd.
 IPR006162; PPantetheine_attach_site. 
Pfam
 PF00501; AMP-binding
 PF00668; Condensation
 PF00550; PP-binding 
SMART
 SM00823; PKS_PP 
PROSITE
 PS50075; ACP_DOMAIN
 PS00455; AMP_BINDING
 PS00012; PHOSPHOPANTETHEINE 
PRINTS