ID A0A1M4VJG8_9BACL Unreviewed; 2091 AA.
AC A0A1M4VJG8;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Non-ribosomal peptide synthase domain TIGR01720/amino acid adenylation domain-containing protein {ECO:0000313|EMBL:SHE68987.1};
GN ORFNames=SAMN05444392_102388 {ECO:0000313|EMBL:SHE68987.1};
OS Seinonella peptonophila.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Seinonella.
OX NCBI_TaxID=112248 {ECO:0000313|EMBL:SHE68987.1, ECO:0000313|Proteomes:UP000184476};
RN [1] {ECO:0000313|EMBL:SHE68987.1, ECO:0000313|Proteomes:UP000184476}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44666 {ECO:0000313|EMBL:SHE68987.1,
RC ECO:0000313|Proteomes:UP000184476};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQVL01000002; SHE68987.1; -; Genomic_DNA.
DR RefSeq; WP_073153966.1; NZ_FQVL01000002.1.
DR STRING; 112248.SAMN05444392_102388; -.
DR OrthoDB; 9765680at2; -.
DR Proteomes; UP000184476; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd05930; A_NRPS; 2.
DR CDD; cd19534; E_NRPS; 1.
DR CDD; cd19531; LCL_NRPS-like; 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; 3.30.559.10; 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; 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; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
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; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 1.
DR SMART; SM01294; PKS_PP_betabranch; 1.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR PROSITE; PS00455; AMP_BINDING; 2.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000184476};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 78..97
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 516..591
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 1542..1616
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 2091 AA; 240102 MW; 3F904521C9032F78 CRC64;
MNQLSEIEQR LINKWNQTEL DLPNVQRVEA LLIEQAMKNP NHLAVVNGAD RLTYGELEQR
SAQLAWVLRE KGVDREKIVG LLVTDSIWMI VAIFAILRAG GAYLPLDPNQ PIERLTELLT
DSQTKLVLKE KDVYLPGYHG EILALESSLL EAENSWSEIA DGDKRDLAYV IYTSGSTGKP
KGVMIEHQSL LNLMIWHQTY HQVTADDRST RYAGFGFDAS VWEIFPYLYA GATIHHVPHS
IRYDIDALHR FYQDNQITIS FLPTQIAEQF MEKENHTLRR LLVGGDRLRR IQTQPYQIFN
HYGPTENTVV TTCWEVTKRE DGMIPIGRPI ANQQVYILDQ QGKPRSIGEA GELCIGGQGL
ARGYLGHESL TKQQFVSHPS NQNRKIYRTG DLARWLPDGQ IEFLGRLDRQ LQIRGNRVEP
AEIEAMLLQY EAVQEVTIVA DQTKPGEIEL TAYIVWKEAG SFKELRDYLA HHLPDYMIPL
AWVEIEQIPL TPNGKIDYKA LPKPSAFHRL HSTFAEPQSS TERRLQHLWQ EILNIPAVGR
EDHFFWLGGH SLAAGRLVAQ IRQEFHVSMS LEDCFANPIL REMANWIESA ETHRLRPVQK
VKPCTTYPLS SVQQRLYALQ QLPGIGCTYH TPVVWEIKGP FDLNRWKQAW KRLMERHEAL
RTSFHWEAGQ LVQKVQDNLS LPFERLELGA DEQVKTCMEY FIRPFQLDQA PLFRLGHLPL
AEQHHVLLFD IHHLLFDGET LKILQQELSI LYHDGFLSSR HWQYRDYVFW EQDDFNQVEH
QKAETFWLEQ LKKPTHHLSL PTDFIRPASQ SFKGKRIAFS IPPALTNACK KLALEQGTTL
YLVLLAVYYL LLAKYSGQSE ITVGTVTDGR NRPEWAKVWG MFVRTLPLRV EISQEMSFVN
WLSKMTAVAL QAFHQDHFSF DSLLRKLKLP SDRSRNPLFD TVFIQQHQTA SLILEGCEVK
TPAIPWNQAM FDLTWEIEER DVIHCTIEYN TSLFQEQTIR RMEKHFTHLL EQIMANPFQT
MKEHRLTTAA EESFILQQLN NTQVAEGDEW LSQTIIDQWT AQVQKHADQI AIASDENNIT
YAELDRLSNQ WAHRLTALGV SDEKIVAILV KPSIEQVIAI LAVLKAGGAF LPIDLNYPSE
RIRALLQDSQ PGWIITSERD SVYSDFAGTI LRVDDAEWTQ NASDALTTKP LPKHLAYVIY
TSGSTGQPKG VMVEHQALHN LTQWHIRQYE VTKDDRSTRL AGSSFDASIW ELFPYLIAGA
TIYIVDDSTR KDVFALQRFI AQHQITICFL PTPLAEPFME LAHPTLRALL VGGDRLRHVP
ATSYAVFNNY GPTENAVVAT CYQVTGAEES IPIGRPIANN RIYIMNDQQQ LQPIGVPGEL
YIAGASLARG YLGRPDLTEL SFLPDSFQAG ERMYRTGDQA QWLPDGTISY LGRMDHQVQV
RGHRVELQEV EQQILRYPQV EQALVLARQN VKEETILHAF VVGDKRIQED LYKFLAERLP
DYMLPAYYTM LDSFPLTPNG KVDEQALRAI PLESVLDREW QPPTLPTERL LAEVWSSLLE
VESIGIDDSF FSLGGDSILA IQVVAELFRH GWKLEVSQLL QYPTIRELAP QLTAEHPIES
KETEESGEVN LTPIQHWFFQ LPFADRNHWN QAVMLTQSER WNDKSIKSAV HDLVIHHDAL
RMCYRFTGNE VTQLNQAESD HCYTIEHLIW DGKQAQKEWI RNEANRLQRS LSLEKGPMLC
FVIFETPNQH FLLMIIHHLI VDGLSWRILL EDFHAAYQAY ERGEAVRLLP KTTSFQAWSR
QLQQYATGDE LIAEIPFWKS VEEKESYPLP KEGSAFWPCR YGETHWIEQT LLAEESKLLL
GAANQAYHTE SNELLLAALG LSVEEWTGRK NVLIELEGHG RESIVQGINL TRSIGWFTTL
YPAHFQWSSP ELKDVILAIK KQLRAIPNKG IGYGVLRYLT PPESRSALSF QLRPEIRFNY
LGKMDKKIQF AGMGKQSALL GNCLSPNAPL APLEIYVMLS GEQLIIQFRY HRLTFSKQTM
EYLLDDYCKN LKRIVQHCCS QNGTHWTVND FSATQLDEQE LRDFLSDLNR P
//
