MYCC_BACIU
ID MYCC_BACIU Reviewed; 2609 AA.
AC Q9R9I9;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Mycosubtilin synthase subunit C;
DE EC=2.3.1.-;
DE Includes:
DE RecName: Full=ATP-dependent serine adenylase;
DE Short=SerA;
DE AltName: Full=Serine activase;
DE Includes:
DE RecName: Full=ATP-dependent asparagine adenylase 3;
DE Short=AsnA 3;
DE AltName: Full=Asparagine activase 3;
GN Name=mycC;
OS Bacillus subtilis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1423;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6633 / PCI 219 / NRS 231;
RX PubMed=10557314; DOI=10.1073/pnas.96.23.13294;
RA Duitman E.H., Hamoen L.W., Rembold M., Venema G., Seitz H., Saenger W.,
RA Bernhard F., Reinhardt R., Schmidt M., Ullrich C., Stein T., Leenders F.,
RA Vater J.;
RT "The mycosubtilin synthetase of Bacillus subtilis ATCC6633: a
RT multifunctional hybrid between a peptide synthetase, an amino transferase,
RT and a fatty acid synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:13294-13299(1999).
CC -!- FUNCTION: This protein is a multifunctional enzyme, able to activate
CC and polymerize the amino acids Ser and Asn as part of the synthesis of
CC mycosubtilin. The Ser residue is further epimerized to the D-isomer
CC form. The activation sites for these amino acids consist of individual
CC domains.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000305};
CC Note=Binds 2 phosphopantetheines covalently. {ECO:0000305};
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000305}.
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DR EMBL; AF184956; AAF08797.1; -; Genomic_DNA.
DR PIR; T44808; T44808.
DR AlphaFoldDB; Q9R9I9; -.
DR SMR; Q9R9I9; -.
DR ESTHER; bacsu-MYCC; Thioesterase.
DR PRIDE; Q9R9I9; -.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.30.559.10; -; 2.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR020802; PKS_thioesterase.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR001031; Thioesterase.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF13193; AMP-binding_C; 2.
DR Pfam; PF00668; Condensation; 3.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF47336; SSF47336; 2.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 2.
DR TIGRFAMs; TIGR01720; NRPS-para261; 1.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis; Multifunctional enzyme; Phosphopantetheine;
KW Phosphoprotein; Repeat; Transferase.
FT CHAIN 1..2609
FT /note="Mycosubtilin synthase subunit C"
FT /id="PRO_0000360850"
FT DOMAIN 771..845
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 2282..2357
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 258..1628
FT /note="Domain 1 (D-serine-activating)"
FT REGION 288..695
FT /note="Adenylation 1"
FT REGION 853..1312
FT /note="Epimerization 1"
FT REGION 1322..1623
FT /note="Condensation 1"
FT REGION 1778..2359
FT /note="Domain 2 (isoleucine-activating)"
FT REGION 1808..2205
FT /note="Adenylation 2"
FT REGION 2375..2581
FT /note="Thioesterase"
FT MOD_RES 806
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 2317
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 2609 AA; 297946 MW; 5E8B8068BFB95CFB CRC64;
MSEFKQQELF WSNMFDAEDR LIAFPSFHMS DSALEHDALN TSNSIHTSLR SDVSLRIMTM
AIIPMAVYLV LLVGIKCLLH KYTGEESIIV GVPTFEDETD EDLRLDQIML LKQNINENST
FKSIFNEFKH TLNDAILHQD VPFDKMVGPL NLNYNSNHLP MIPAIVSLDQ IHLIHFKETA
ASDTLFQFDI KNDAIHLKVT YNEQAYDRQY MMQVIEHLNR LFSIILFQPD ITISQLNILT
DTEINTFKDY NQTAAEYPRE KTIHQLFEEQ ANRTPDQVAV VYEENQLTYQ ELNEKANQIA
RTLQSEGVHP DQPVGIMAER SLEMIVGLFG ILKAGGAYVP IDPTYPEERI RYILEDSDTK
LLLVQHHLRE KVPFTGKVLD MEDPQTFSED GSNLESISGP NQLAYVIYTS GSTGKPKGVM
VEHRSVINRL VWMQENYPLD ERDAILQKTA ITFDVSVWEL FWWSIVGSKV VLLPNGGEKN
PELILDTIEQ KGVSTLHFVP AMLHAFLESM EQTPSGKLKR KLASLRYVFA SGEALTPKHV
DGFQRIITPV SHAQIINLYG PTEATIDVSY FECEADKRYN SVPIGKPISN IQLYILQAGY
MQPVGVAGEL CIAGDGLARG YLNRPELTAE KFVKNPFSAG ERMYRTGDLA RWLPDGNIEY
LGRIDHQVKI RGYRIETGEV EAALFHIPSI QESIVLAQEI NEEISLCAYY TANDTLTAGE
LREHLSRQLP SYMIPAYFIQ LKRMPLTLNG KIDRRALPSP RENLTGMDYT APRTELEKIL
AATWESVLGL ERVGVSDHFF ELGGDSIKSI QVSSRLYQAG YKFEIKHLFK YPTISELVPY
VEPVTRVAEQ GEIKGPALLT PIQHWFFDQR YPDLHHYNQA VMLYWKEGLN VPMLREVMRK
IVEHHDALRM VYVPAKHGYE ARNREIDEGD LFSLEVFSLL EENNVAQTIE TLSNEIQQSI
QLAEGPLIKL GLFQCQDGDH LLIVAHHLVI DGVSWRILIE DIAAAYEQLL NGEAIQLPKK
TDSYLLWAEQ LKRYAESPEF EMKNQYWFQH EHIPLPKLPK DNEQEIGLAE DRETIIVQWT
AEETERLLKN AHRAYTTEMN DLLLTGLGIA IHRWTGHEDI LIHLEGHGRE SIIPDLDISR
TVGWFTSQYP VFLPIKADHD ISQRIKTVKE HLRKIPQKGI GYGIIKYLSD HREDREFTGQ
PEISFNFLGQ FDQDLQNGSI EVSPYSSGKI ASDKHPLTYA LDINGMISNG RLSLAISYCG
KQYHKETMET CADLLKSSLR QVIEHCTAQD QVQLTPSDIS LKEISIDELD QFVQQAQHLG
EIENIYPLTP MQKGMLFHSL IDSASGAYFE QAAFDLKGLL DIEAFMMSLS QLAKRYDILR
TQFYTEWKEQ PLQIVLRHKP IETVVEDIRD MNVDQRSEFI AAFARKDKER GFNLIRDALM
RVSILRTDEE KARLIWSFHH ILMDGWCLPL ITKEVFETYY AIIERRQPKR DAVTPYRQYI
EWLDEQDHEQ AAVYWRDYLD DYEGQTVLLK EPFSDQARGY QKQKLACRLG KQLTEEIKRA
ASQHHVTVNT WMQTAWGLLL QRYNGTQDVV FGTVVSGRPA DIPGIESMVG LFINTIPVRV
CAQPEMTVAQ VLKMNQEHAL ASQPYDTFPL YEIQAQTEQK QQLINHIMVF ENYPVEKQME
HMKRDHDVLD ISDFHLEEHT HYDFNFIVMP AEDMEMHFVY NANVYDQATV ERIQAHFMEI
IKQMVNDTAV HVQELDILSE DERSLLIEKF NDTATEYPKE KTIYQLFEEQ AARTPEQIAI
VFEDQKLTYR QLNEQANQLA RTLRAKGVRS DRTAAIISDH SIELVVGILA VLKAGGAYVP
IDPDYPEQRI QYILNDSKTE IVLTQSHLQQ RLAHEGTIVL LDDENSYHKE RSNLERISNI
KDLAYVIYTS GSTGKPKGVL IEHQGLTNYI WWADRVYVKG EKTTFPLYSS IAFDLTVTSI
FTPLISGNAI IVYGDKDRTT LLSSIIEDSR VDIIKLTPAH LQLLKEMNIS PECTIRKMIV
GGDNLSTRLA QNISEQFQDQ IEIFNEYGPT ETVVGCMIYL YDPKKDRQES VPIGTAAANM
NIYLLDTGMK PVPIGVPGEM YISGAGVARG YLNRPDLTAE KFVEHPFAAG ERMYKTGDAA
RWMPDGHMEY LGRIDHQVKV RGYRIELGEV EAALLLVESV KEAVVIAVEE EGSNQLCAYV
TGDESLKTLQ LKQQLQNKLP AYMIPAYFVQ IEEMPLTANG KIDREALPAP DGNMLAGTEY
AAPRTLIEKQ LAEIWKEVLA HSELGIKDNF FDVGGHSLKV LQLVDQINKV MGIKLHYHVV
YEAPTIETMA HAIQAAALPS KTENVFVKLN QNGSIPVFCF PPLIGYGLVY NEMANRLDGD
CVVYAADFTE DPSYKKPIID RFAESMIDIQ EQGPFVLLGY SSGSNLAFEV AKALEQRGRT
VSDVIMLDSQ ITTSVTHLSE KEVEEIIHLN LDIIPVYYRE LLTIPSIKEK IRGYLAYHNQ
LINSGTINAN IHHLLCDDMT ERGWTHSTAH NYKEYELKGD HVTIFDPQYI EENMSTIRSI
MKCIEEQQLG ELVPHEQLSY MSRTKSDRT
