ID B7I0Z5_BACC7 Unreviewed; 2681 AA.
AC B7I0Z5;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Linear gramicidin synthetase subunit B {ECO:0000313|EMBL:ACJ82785.1};
DE EC=5.1.1.- {ECO:0000313|EMBL:ACJ82785.1};
GN OrderedLocusNames=BCAH187_C0023 {ECO:0000313|EMBL:ACJ82785.1};
OS Bacillus cereus (strain AH187).
OG Plasmid pAH187_270 {ECO:0000313|EMBL:ACJ82785.1,
OG ECO:0000313|Proteomes:UP000002214}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534 {ECO:0000313|EMBL:ACJ82785.1, ECO:0000313|Proteomes:UP000002214};
RN [1] {ECO:0000313|EMBL:ACJ82785.1, ECO:0000313|Proteomes:UP000002214}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187 {ECO:0000313|EMBL:ACJ82785.1,
RC ECO:0000313|Proteomes:UP000002214};
RC PLASMID=Plasmid pAH187_270 {ECO:0000313|Proteomes:UP000002214};
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
RL Submitted (OCT-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}.
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; CP001179; ACJ82785.1; -; Genomic_DNA.
DR SMR; B7I0Z5; -.
DR KEGG; bcr:BCAH187_C0023; -.
DR HOGENOM; CLU_000022_11_0_9; -.
DR Proteomes; UP000002214; Plasmid pAH187_270.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; 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:0019752; P:carboxylic acid metabolic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic 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; cd12117; A_NRPS_Srf_like; 1.
DR CDD; cd08953; KR_2_SDR_x; 1.
DR CDD; cd19531; LCL_NRPS-like; 1.
DR Gene3D; 3.30.300.30; -; 3.
DR Gene3D; 3.40.50.980; -; 2.
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; 1.
DR Gene3D; 3.40.50.12780; N-terminal domain of ligase-like; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 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_com.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR013968; PKS_KR.
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; 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; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00824; PKS_TE; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 3.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
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 Isomerase {ECO:0000313|EMBL:ACJ82785.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Plasmid {ECO:0000313|EMBL:ACJ82785.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 250..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1279..1354
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2327..2401
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2681 AA; 304305 MW; 8CA73A5EE74F0C6E CRC64;
MLSTRKNLHA NLVRIQGKRV DLKKIERQVA KVSFIEQCAV IARKQDDGEY LLTAFVVSEK
AAAKEELQLL EVLPPKSQII SMSSLPLTKE GTIDRQQLMS LLCITADEEM RLQQSYGKEK
MAITYEEVFR LPNVNHVYDV MKVKETSQKV VSREKQAKEH FAQHIPAYMV GEDLTQFDMS
QEPKTLVEVI HNAAKNYGNH GITFIDEHGK TEFLTYKMIL MEAERMLKGL RAFQLQPQDK
IIFQMNNDKV FVITFWACVL GGFIPVPITV PKMFTQRTNE ADTLYNIWRA LEKPYIVTNE
TLQDSMTQLL DCYDLDAAKY LAFEKIQQEE PDQNWHVAQS EDDAILLFTS GSTGNPKGVV
QKHRSILTRE ISTSKYNHFS AHDIALNWMP LEHVGGIVMF HIKDTYLGRN QVQVRTQYVL
SEPTRWLDLI TTYKATITWA PNFAFALINK EIENGVKGNW DLSSMEFIVN AGEAINGYTA
KKFLQVLSPY GLPEDAMIPV WGMSETCSGV VYNKAFRSDG TKGLFIVDKQ SLEGIIQEGN
NVEDTITFVN LGKPIYGVSI RIANQDNETV AEGVIGRLQI KGKNVLEGYY QNEEANKECF
TEDGWYDTGD LAFIKDGCMA ITGRGKDIII INGVNFNGTE IEYVVEQVAG VKTSFVAACA
VRDDQLDTDE LAIFYSTMCA NDEEIREQIQ EIDQTIIEKF GVKASYIIPV EEEEIPKTNI
GKIQRTKLSN QFRLGYYEKL SKEIDILLQN DRTIPAWFYE QGFVRKETEI TFNPKETRKI
VIVGESTAFV TTIKRKLEEV GHHCYLVGNR EAYLSILKQE EIDDVINLLN YEKQDADGNE
IEKIRNANEN GIFFISETIK ACGKEKNLRI FTVTNNCEYS NIMKNKYHFG TLDGFSRSVN
LELPNLMCIR IDLDVSENDV NSIIKEIAAI HRDDKVVYRE GKRYVDSLQP IDMPLSLQNE
IALIKDGIYV VTGGLGGIGK EVCKLLLQQF SAKLFIVGRT ALSTSPTHLA SLEELQGFSK
DVHYIDGDLS DAAFVASISA KVEEIWGTEL DGILHLAGAG NLEEHWSEID SHWCTTESKA
YYEEMFAAKV FGTVNLFQLI EGKKDALFLH FSSVNSYFGG ASFTAYAAAN NFQDTFCQYV
SNQGYKNAIC INWSMWYDIG MSRNNTNNEL MAEKGFLLLP MKQAVYSLLA VLRTGVNNIF
VGLDASKSNI RKSMKQKKEL GLKAIVYHTD EVSDLSIEAK KHVSFLKVDE IPIDEKGCVQ
IGKLQDLHKN VGKTEMFQEP QSEAEKTLAK IWRDVLKANK IGRDSNFFEL GGHSINATQL
VSKIYSVCRV RMPLKNVFQY TTLATMARVL EELLVSAVDE VAVTTERIPK ILPRTYYDLS
YSQQRIYFLS TMEKETNYYN ILGAWDIYGK LDVTLFEKAI QLLMKKHHSL RATFEIVDGK
PVQIIHDDME IPVQFIDLTV MPEGLRIEEV DELMLKESKR VYNLANGPLM HCTIVKIKEG
EHVLLIGQHH IISDGWSLGI FVKELNEMYD AFVQHKPVAE TPSTISIMDF TAWHNSKVDE
DQDDRQYWLQ RFEGELPTLE LPTDRQRPLL KTYHGDTLSY KVNSQLHQKL KDFSHANGVT
MFMTLLTAYN IMLNKLTNET DIVVGSPVAG RNEPESKDLI GMFVNTLALR SHLGDNPTVD
VLLKQIKQNT LEAYNHQDYP FDKLVDDLDP HRDLSRTPIF QVMMGYMNMP LMVAFREAEV
RERFVRHKVA RFDLTLHVFE DEDQMKIFFE YNTDLFDEST IMRWQNHFET LLQEIVSNPT
KRISELNILT NEEKYEILEM NNNSTEYPQH ESVAEIFRET KIKHQAKLAI TYKDRKLTYA
ELSEKANALA HTLKRRGVAQ HDVVGIVAER SPETIIGILA ILKVGAIYLP IDPKLPQLTL
QHIWRDSGAK VLLGKNETTV EVGKEVPFVD IEGDKGKQEE LVCPISPEDT AYIMYTSGST
GKPKGVMVTH RNIVRLVKNT NFVSLQEQDV LLQTGSLTFD AATFEIWGAL LNGLTLHLVE
DYVILDGEAL QEEIQQNKAT IMWVSAPLFN QLADQNPAMF TGIKQLLIGG DVLSPKHINK
VMDHCAPINI INGYGPTENT TFSTSFVIDQ MYQDSIPIGT PIANSSAYIL DVHQNIQPIG
VVGELCVGGD GVAKGYVNLE QLTEERFIAD PFLKGSTMYR TGDYVKLLPN GNIQYIGRVD
NQVKIRGFRI ELEAIMNTLK QCESIKDVIV VVQEQNGYKT LVAYVVGEES LSIETVRAYA
KKHLAEYMVP SQFIFIEEIP LSINGKVQYS KLPKVQEVLH KKVETLLPEN RLEEIILRVY
RDVLEKEDFG VTDSFFAYGG DSLLSIQVVS MLKKEEIAVD PKMIFMHTTV RELAKACENR
PVMEETKRTE KDYLIQMREG SEEDSCIIFA PPAGGTVLGY IELARYFEGI GNVYGLQAPG
LYDDEEPTFL DYDELVQVFL RSIEGTYRPG QDYLGGHSLG GHIAFGMCCE LIKQGKAPKG
LLILDTTPSL QVVKGAKDEK IAEEDFKMMV LAAGIGNMMG VDPEELKQLS YEEAKTRVVA
VAQKDEKLKT FINETYLDKY LKLQIHSLLM SRTLELEKTQ LDIPIKVFKT QFHTEELVER
FDAWHNYTNQ ACTFIDIPGT HTTMMRLPHV KEVAKKIEEQ L
//