UniProt: B6E114

Database: UniProt
Entry: B6E114_BACIU

LinkDB:  B6E114_BACIU 
Original site:  B6E114_BACIU

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Ontology (7)   
   GO (7)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (25)   
   InterPro (15)   
   Pfam (5)   
   PROSITE (3)   
   SMART (2)   
All databases (33)   

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ID   B6E114_BACIU            Unreviewed;      2619 AA.
AC   B6E114;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=Bacillorin synthetase C {ECO:0000313|EMBL:ACI22673.1};
GN   Name=bacC {ECO:0000313|EMBL:ACI22673.1};
OS   Bacillus subtilis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423 {ECO:0000313|EMBL:ACI22673.1};
RN   [1] {ECO:0000313|EMBL:ACI22673.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=916 {ECO:0000313|EMBL:ACI22673.1};
RA   Luo C., Chen Z., Liu Y.;
RT   "Cloning, Sequencing, and Function Characterization of Bacillorin Operon in
RT   Bio-control Bacillus subtilis 916.";
RL   Submitted (SEP-2008) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; FJ194462; ACI22673.1; -; Genomic_DNA.
DR   ESTHER; bacsu-q6yk39; Thioesterase.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR   GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR   GO; GO:0044550; P:secondary metabolite biosynthetic process; IEA:UniProt.
DR   CDD; cd05930; A_NRPS; 1.
DR   CDD; cd19543; DCL_NRPS; 1.
DR   CDD; cd19534; E_NRPS; 1.
DR   Gene3D; 3.30.300.30; -; 2.
DR   Gene3D; 3.40.50.980; -; 4.
DR   Gene3D; 1.10.1200.10; ACP-like; 2.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR   Gene3D; 1.10.287.490; Helix hairpin bin; 1.
DR   Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 3.
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_com.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR001242; Condensatn.
DR   InterPro; IPR010060; NRPS_synth.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR020802; PKS_thioesterase.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 2.
DR   NCBIfam; TIGR01720; NRPS-para261; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
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; SM00823; PKS_PP; 2.
DR   SMART; SM00824; PKS_TE; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 5.
DR   PROSITE; PS00455; AMP_BINDING; 2.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   3: Inferred from homology;
KW   Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}.
FT   DOMAIN          774..848
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          2289..2364
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   2619 AA;  299327 MW;  6389DE25B7D15F09 CRC64;
     MSEFKQQELF WSSMFDAEDR PSAIPSFQMS DSTIEHEAPS APNRIHSSLS SDVSLRIMKM
     TNKSPMAVYM VLLVGIECLL YKYTGEEGVI VGVPTFEDET DEDLRLDQVM LIKQNINADG
     TFKSIFNEFK HTLNGAILHQ HVPFDKMAGP LNLNYDSNHL PMIHTIVSLD QLHPIRFIET
     AASDTLFQFS IENDSIHLKL TYNEQAYDRQ YMIQVIEHVN RIFSILLFQP DLMIRQLNIL
     SDSETNQLIA YNQTAAEYPR EKMIHQFLEE QAERTPDQTA VVYEDSRLTY RELNERANQL
     ARTLQSEGVQ PDQPVGIMAE RSLDMIVGIF GILKAGGAYV PIDPGYPEER VRYILEDSDT
     KLLLVQNQSR ERVPFTGKVL DMKDPQNFCE DGSNVEPAAG PDHLAYVIYT SGSTGKPKGV
     MVEHRSVINR LVWMQEKYPL DERDAILQKT AITFDVSVWE LFWWTISGSR LVLLPNGGEK
     NPELILDTIA QKGVSTLHFV PAMLHAFLES MDQKPSGMLK QKLASLRHVF ASGEALKPVH
     VAGFKRIITS VSQAQIINLY GPTEATIDVS YFDCQTEEMY ASIPIGKPIS NIQLYILHAD
     LEHMQPIGVA GELCIAGDGL ARGYLNRPEL TAEKFVNHPI ASGERIYRTG DLARWLPDGN
     IEYLGRIDHQ VKIRGYRIEI GEVEGAFFQL PAIKEAIVIA REIEGETSLC AYYTAQHALT
     AGELREELSR QLPSYMIPAY FVQLEEMPLT FNGKIDRKSL PSPRENLTGM NYEAPRTELE
     KILAAVWESV LGLERVGISD HFFELGGDSI KSIQVSSRLY QAGYKFEIKH LFKYPTISEL
     VPYVEPVTRI AEQGEIKGRA LLTPIQHWFF DQKYPELHHY NQAVMLYWNE GLDESKLRDV
     MKKITEHHDA LRMVYVPTED GYEARNRGID EGDLFSLEVI SLREEKNVSQ TIETISNEIQ
     QSIHLAEGPL MKLGLFRCQE GDHLLIAVHH LVIDGVSWRI LLEDIAAAYE QLQNGEAIRL
     PKKTDSYLLW AEQLNRYAES QEFEAENQYW FRQKHNPQLT LPKDNEQETG LAKDKETVIV
     QWTVEETERL LKNAHRAYST DMNDLLLTGL GTAIHRWTGC EDILIDLEGH GRESIIPDLD
     ISRTVGWFTS LYPVSLQIKA DQDIPQRIKT VKENLRQIPQ KGIGYGLIKY LSDHPKAHEW
     TGHPEIRFNY LGQFDQDVRN GKMEVSPYSS GKTASDNRPL TYTLDINGMI SDGRLSLAIS
     YCGKQYQRET MEACADLLKS SLQQVIAHCD AQNQIHLTPS DISLKGITIG ELDQFVQQTS
     HLGDIENIYP LTPMQKGMLF HSLIDSASEA YFEQAAFDLK GFLDIDAFRM SLAHLAEKYD
     ILRTLFYTEW KDQPLQIVFR QKPIETAVED IRSMNSHQRS EFIADFARRD KARGFNLTRD
     ALMRVSILRT EEDQARLIWS FHHILMDGWC LPLVTKEVFE TYYAILEQRQ PKRGAVTPYS
     RYIEWLDQQD HKQASAYWRN YLEGYEGQTV LLQEQTSDRA KGYEKGEHEF RLGKRLTDEI
     KRAASRQQVT VNTWIQTAWG LLLQRYNGSQ DVVFGTVVSG RPAEIPGIET MVGLFINTIP
     VRIHTQPEMT AAQVLKMNQE RALASQKYDT FPLYDIQAQT EQKQQLINHI MVFENYPVEK
     QIEHMKQDDN ALDILDFHME EHTHYDFTFI VMPDGEIDIR FVYNRDVYDQ ASVERMQTHF
     IQIMKQMADD QEIRVQDLDI VTADERSLLI DKFNDTAAEY PKGKTIHQLF EEQAERTPEQ
     AAIVFEDKKL TYRLLNERAN QLARTLVAKG LQAEELVGIM AERSPEMVIG ILAILKAGGV
     YVPIDPDYPK ERIHYMLEDS NVSILLLQHH LLEGTDYQSH TVFLDDPSSY GAEASNLNLN
     VMPNQLAYVI YTSGTTGNPK GTLIEHKNVV RLLFNNKNVF DFNASDTWTL FHSFCFDFSV
     WEMYGALLYG GKLVIVPKQI AKNPERYLQL LKSEAVTILN QTPSYFYQLM QEERADPESN
     LNIRKIIFGG EALNPSFLKD WKLKYPLTQL INMYGITETT VHVTYKEITE REIDEGRSNI
     GQPIPTLQAY ILDEYQRIQV MGIPGELYVA GEGLARGYLN RPELTAEKFV EHPFAAGEKM
     YKTGDVARWL PDGNIEYLGR IDHQVKIRGY RIEIGEVEAA LLQSESVKEA VVIAIEEEGS
     KQLCAYLSGD DSLNTAQLKS HLLNKLPAYM IPAYFVQMEK MPITANGKID RKALPAPEGN
     RLTGTEYEAP GTLIEKQLAE IWKNILALSD PGIKDNFFDV GGHSLKVLQV IHQINDRMGI
     KMHYQAVYDF PTIETMARAI QAAVFESKTD NVFVKMNQNG LIPVFCFPPL IGYGLVYNEM
     AKRLDGRCTV YAADFLEEPS YEQEIVDRYA ESMIGIQEQG PFVLLGYSSG SNLAFEVTKA
     LEKRGRIVSD IMMLDSKRAV SVNYFSEEET EEIIHRNLDI IPDYYRELLT IPSIKDKIRS
     YLTYHNKLIN SGAVNANIHH FLCGELTDRG WKQSTAQHYL EYKLKGDHVT IFDPHNIEEN
     TDTIRSIIKR IEERHHHGLV LEEQLSMGSF AGDTKFDKM
//

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