ID H3SN24_9BACL Unreviewed; 1917 AA.
AC H3SN24;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Bacitracin synthetase 3 {ECO:0000313|EMBL:EHQ59531.1};
DE Flags: Fragment;
GN ORFNames=PDENDC454_24859 {ECO:0000313|EMBL:EHQ59531.1};
OS Paenibacillus dendritiformis C454.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1131935 {ECO:0000313|EMBL:EHQ59531.1, ECO:0000313|Proteomes:UP000003900};
RN [1] {ECO:0000313|EMBL:EHQ59531.1, ECO:0000313|Proteomes:UP000003900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C454 {ECO:0000313|EMBL:EHQ59531.1,
RC ECO:0000313|Proteomes:UP000003900};
RX PubMed=22461558; DOI=10.1128/JB.00158-12;
RA Sirota-Madi A., Olender T., Helman Y., Brainis I., Finkelshtein A.,
RA Roth D., Hagai E., Leshkowitz D., Brodsky L., Galatenko V., Nikolaev V.,
RA Gutnick D.L., Lancet D., Ben-Jacob E.;
RT "Genome Sequence of the Pattern-Forming Social Bacterium Paenibacillus
RT dendritiformis C454 Chiral Morphotype.";
RL J. Bacteriol. 194:2127-2128(2012).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHQ59531.1}.
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; AHKH01000121; EHQ59531.1; -; Genomic_DNA.
DR STRING; 1131935.PDENDC454_24859; -.
DR OrthoDB; 9765680at2; -.
DR Proteomes; UP000003900; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.980; -; 4.
DR Gene3D; 1.10.1200.10; ACP-like; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
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; IPR020459; AMP-binding.
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; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 2.
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; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 1.
DR PRINTS; PR00154; AMPBINDING.
DR SMART; SM00823; PKS_PP; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000003900}.
FT DOMAIN 980..1055
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT NON_TER 1917
FT /evidence="ECO:0000313|EMBL:EHQ59531.1"
SQ SEQUENCE 1917 AA; 218079 MW; C5989AEE3A732BC0 CRC64;
MRENTNKQYG LTQAQRRIWF MEIMNPGTSI TMLSATYQIT GKIDTQLLEQ AAAEIVKTYD
AFRIRISGDL QNPTQWFEEP ENVQARISRL EIDTTEQFYA WVKEVSEKPA SVFDEYLHQF
TIIHFANGQV WLNLTINHII ADGLSVTALL HAVMEKYLEL RKGISSSYQA PSYLDYIFAE
REYEQSQRYQ KGKEYWLTKY STLPETTGIK SYPPFAIGSE SNKRAITLDG SRYERILAFS
EQYQVSLYTL FLSAMYALLY KLTDSTDIPV GTVFANRTSK KEKETIGMFV STVATRIRLN
PDGHVLSLIQ SVSKENTADL RYQKYPYNQL IQDLREQHGR NDLSGLFRTS LEYLPLKIVE
YEEIKVRLEA HFARHEMDDL LLRFDHMLSE GHVILHASYR TGLFETAEID RIMEQYVTVL
DQFLQTPELP VREISLLSDE ERHRILNVFN PPVAGLSEGE AFHRYVEKFA REIPDHPAVV
YMDKQLTYGE LNERAERLAS LLREQGVGRE TITGIWAERS VELLVGVLAV WKAGGAYVPL
DPDYPAERIE YMLSDSEASV LLTQRHLLER AEGWLADDRL KLQAVYAMDD EQIYNGDALA
GEFESAGSAP QDLAYVIYTS GTTGRPKGVM IEHGSLVSTA DAYRREYRLD QFPVRLLQLA
SFSFDVFVGD IARTLYNGGT MVIVPKDDRI DPNRLYGWIR DQNITVFEST PALILPFMQH
IYEEGLDVSS MQLLITSSDA CSVTDYRLLQ ERFGGQFRII NSYGVTEAAI DSSFYDEPLD
KLPPSGHVPI GKAWLNARFY IVDAALKPVP VGVPGELVIG GAGVARGYWN RPDLTAEKFA
DSPFVPGERL YRTGDLARWL EDGNVDFIGR IDYQVKIRGF RIELGEIETA LLRFPGVKQA
VVTDRTDEQG QKYLCGYVAG DASLQLSDLL SQLKQELPAH MVPARLVSLD KLPLTPNGKI
DRKALPEPTG EIEAGREHVA PRTTLETRLA LIWQQVLGIA RVGVQDDFFD LGGHSLRASA
LVSKIRKELQ VEVPLRDVFR YITIEQLAQR IGGLRQQEAY EITKAAEAEY YPVSSEQKRL
YVLRQLDGAE RSYNMSAALL LEGKLDRMRA EHAFRALIQR HETLRTGIEQ VQGELVQRIY
DEVEFAVDYF HASEREAEQV VEAYYRPFDL TKPPLLRIGL IEVAEDRHIL LFDMHHIVSD
GISTALLFDE FSRLYRGEEL APLGIQYKDY AVWQHSEAYG QMLQPQKEYW LEQLSGELPV
LELPTDFPRP AVQSFDGRTV KFYIGKERTE KLKELAARTG TTLYMVLLSA YSILMHKYSG
QEDLIVGTPI AGRTQDEVQP IVGMFINTLA IRSRPERSKP YLSYLEEIKD ITLGAFEHQN
YLFEDLVESL HIPRATGRNP LFDTFFSLQN TENEQIVIEG LEQSFYPLEN RTSKFELLMD
ISELDGQLEC RLEYATALYK QETAERFARH YDKLLETIAA APDGDIASLE MLTEEEIRLL
VRGFNDSEAD YPRQQTIHGL FEEQAELYPD NVAAVMNERQ LTYRELNERS NRLARKLRET
GVEADQLVAI LAERSLDMVV GILAILKAGG AYVPVDPDYP EERIRFMIED SGAPLLLIQK
HLHEKTDFAG TRLELDDFVW GDRGADSEGA LDASNLEPIS GPGNLAYVIY TSGTTGRPKG
TLIEHKNVVR LLFNDKNLFD FGPSDTWTLF HSFCFDFSVW EMYGALLYGG KLVIVPPLTA
KNPADFLALL GREQVTILNQ TPTYFYQLLR KVLADHPYDL RIRNVIFGGE ALSPLLLKGF
KTKYPETKLI NMYGITETTV HVTYKEITWV EMEAAKSNIG KPIPTLRVYI LDENRRPVPI
GVAGEMYVAG EGLARGYLNR PDLTAEKFVD SPFAEGEKLY RSGDLAAWLP DGNIEYL
//
