Q45563 (Q45563_BACSU) Unreviewed, UniProtKB/TrEMBL

Names and origin

Protein names

Submitted name:
Fengycin synthetase EMBL AAB00093.1

Gene names

Name:

fenB EMBL AAB00093.1

Organism

Bacillus subtilis EMBL AAB00093.1

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	1274 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Phosphopantetheine RuleBase RU000721
Technical term	3D-structure PDB 2CBG PDB 2CB9
Gene Ontology (GO)
Biological process	biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	acyl carrier activity Inferred from electronic annotation. Source: InterPro cofactor binding Inferred from electronic annotation. Source: InterPro hydrolase activity, acting on ester bonds Inferred from electronic annotation. Source: InterPro ligase activity Inferred from electronic annotation. Source: InterPro phosphopantetheine binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequences

	Sequence		Length	Mass (Da)
	Q45563 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 068DA342F321CE95	FASTA	1,274	143,630
	10 20 30 40 50 60 MVKTKKIKNV YPLSHMQEGM LFHSFLHKEE GAYVEQSLFT IKGSLSYEIF QRSIQAIIDR 70 80 90 100 110 120 HDIFRTVFLP HVPNLSGPRQ VVMTERNFHL HTEDISSLQT NEQNDYIEQF KEKDKKKGFD 130 140 150 160 170 180 LQKDMLMRIS LLKTAENEHV CVWSHHHILM DGWCLGIILQ EFMQIYQSIH TGNHLALEPV 190 200 210 220 230 240 RPYSTYISWL TKQDKETAAD YWRAYLKNYS TPSQLPRVTD REAKEGYYRE ELIFTLNQKL 250 260 270 280 290 300 TDKLKETAKQ TGVTLATFIQ TVWGVMLQRY NRTDDVVFGA VVSGRPSEIP GVESMIGLFI 310 320 330 340 350 360 NTVPVRVKTG KEETFAELLS RCQQDMLDAE PFTCHPLFDI QANTALKQEL IDHIIVFENY 370 380 390 400 410 420 PLQQKMADSA DQIDSPLQID NVKVSEQSGY NFNLVVAPGD ELVIKFSYNA HVYDAAWMTC 430 440 450 460 470 480 IQRQLTQALQ AAADHPDIPV ADFSFLDPKE KEQILTQCND TSTAYPKNKT VIDIFREQTV 490 500 510 520 530 540 KTPDQTALVY GNRSISYREL DQKSDALART LYENGLRRNG TAGILAGHSP EFIISVLAVL 550 560 570 580 590 600 KAGGTYLPLD AELPPERISY MLSETKAAIL IVQKGLEPNT AFAGTFISAD AEAMIEEHTK 610 620 630 640 650 660 PLEIVTGPDD LAYIMYTSGS TGRPKGVMIT NRNVVSLVCN SNYTSASVND RFILTGSISF 670 680 690 700 710 720 DAVTFEMFGA LLKGATLHII DKSTMLTPDR FGAYLIENNI TVLFLTTALF NQLAQAQADM 730 740 750 760 770 780 FHRLHTLYVG GEALSPELIN AVRRACPNLS LYNIYGPTEN TTFSTFFEIK RDYATPIPIG 790 800 810 820 830 840 KPISNCTAFI LDAKGCLLPI GVPGELCVGG DGVAKGYLNR DDVTAAVFSP DPFIPGERIY 850 860 870 880 890 900 RTGDLARWLP DGNLEYISRI DRQIKIRGKR IEPAEIEARL LEIEGVREAA VTLLETDGEV 910 920 930 940 950 960 QLYTHYVSDE SRNEKEIRAA LARVLPDYMI PQRWVRVDRM PLTGNGKINR SALPVPENES 970 980 990 1000 1010 1020 ENRQDLTPPR NWVEQELTQI WKSVLGVKTI GIHDDFFALG GHSLKALQVI HMLKHHQHVD 1030 1040 1050 1060 1070 1080 IPIDVLFENP TIAQLAEKLY SNQLSAAGEQ HVIQLNQQGG KNLFCFPPIS GFGIYFKDLA 1090 1100 1110 1120 1130 1140 LQLNHKAAVY GFHFIEEDSR IEQYVSRITE IQPEGPYVLL GYSAGGNLAF EVVQAMEQKG 1150 1160 1170 1180 1190 1200 LEVSDFIIVD AYKKDQSITA DTENDDSAAY LPEAVRETVM QKKRCYQEYW AQLINEGRIK 1210 1220 1230 1240 1250 1260 SNIHFIEAGI QTETSGAMVL QKWQDAAEEG YAEYTGYGAH KDMLEGEFAE KNANIILNIL 1270 DKINSDQKVL PNKH

References

[1]	"Transposon mutagenesis and cloning of the genes encoding the enzymes of fengycin biosynthesis in Bacillus subtilis." Chen C.L., Chang L.K., Chang Y.S., Liu S.T., Tschen J.S. Mol. Gen. Genet. 248:121-125(1995) [PubMed: 7651334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE. Strain: F29-3 EMBL AAB00093.1.
[2]	"The thioesterase domain of the fengycin biosynthesis cluster: a structural base for the macrocyclization of a non-ribosomal lipopeptide." Samel S.A., Wagner B., Marahiel M.A., Essen L.O. J. Mol. Biol. 359:876-889(2006) [PubMed: 16697411] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 1043-1274.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

L42523 Genomic DNA. Translation: AAB00093.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2CB9	X-ray	1.80	A	1043-1274	[»]
2CBG	X-ray	2.50	A	1043-1274	[»]

ProteinModelPortal

Q45563.

SMR

Q45563. Positions 1045-1263.

ModBase

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Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Family and domain databases

InterPro

IPR010071. AA_adenyl_domain.
IPR009081. Acyl_carrier_prot-like.
IPR020459. AMP-binding.
IPR020845. AMP-binding_CS.
IPR000873. AMP-dep_Synth/Lig.
IPR001242. Condensatn.
IPR006163. Phsphopanteth-bd.
IPR006162. PPantetheine_attach_site.
IPR001031. Thioesterase.
[Graphical view]

Gene3D

G3DSA:1.10.1200.10. ACP_like. 1 hit.

Pfam

PF00501. AMP-binding. 1 hit.
PF00668. Condensation. 1 hit.
PF00550. PP-binding. 1 hit.
PF00975. Thioesterase. 1 hit.
[Graphical view]

PRINTS

PR00154. AMPBINDING.

SUPFAM

SSF47336. ACP_like. 1 hit.

TIGRFAMs

TIGR01733. AA-adenyl-dom. 1 hit.

PROSITE

PS50075. ACP_DOMAIN. 1 hit.
PS00455. AMP_BINDING. 1 hit.
PS00012. PHOSPHOPANTETHEINE. 1 hit.
[Graphical view]

ProtoNet

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Entry information

Entry name

Q45563_BACSU

Accession

Primary (citable) accession number: Q45563

Entry history

Integrated into UniProtKB/TrEMBL:	November 1, 1996
Last sequence update:	November 1, 1996
Last modified:	September 21, 2011
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)