ID A0A3D9KHG6_9BACL Unreviewed; 2627 AA.
AC A0A3D9KHG6;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Yersiniabactin nonribosomal peptide synthetase {ECO:0000313|EMBL:RED85336.1};
GN ORFNames=DFP98_10441 {ECO:0000313|EMBL:RED85336.1};
OS Cohnella phaseoli.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX NCBI_TaxID=456490 {ECO:0000313|EMBL:RED85336.1, ECO:0000313|Proteomes:UP000256977};
RN [1] {ECO:0000313|EMBL:RED85336.1, ECO:0000313|Proteomes:UP000256977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7287 {ECO:0000313|EMBL:RED85336.1,
RC ECO:0000313|Proteomes:UP000256977};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- PATHWAY: Antibiotic biosynthesis; bacillaene biosynthesis.
CC {ECO:0000256|ARBA:ARBA00004789}.
CC -!- SIMILARITY: Belongs to the ATP-dependent AMP-binding enzyme family.
CC {ECO:0000256|ARBA:ARBA00006432}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the NRP synthetase
CC family. {ECO:0000256|ARBA:ARBA00029443}.
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:RED85336.1}.
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DR EMBL; QRDZ01000004; RED85336.1; -; Genomic_DNA.
DR Proteomes; UP000256977; Unassembled WGS sequence.
DR GO; GO:0016746; F:acyltransferase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR CDD; cd19535; Cyc_NRPS; 2.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 2.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 1.
DR Gene3D; 1.10.10.1830; Non-ribosomal peptide synthase, adenylation domain; 1.
DR Gene3D; 3.30.559.30; Nonribosomal peptide synthetase, condensation domain; 2.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR001227; Ac_transferase_dom_sf.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR014043; Acyl_transferase.
DR InterPro; IPR016035; Acyl_Trfase/lysoPLipase.
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; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR016036; Malonyl_transacylase_ACP-bd.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR016039; Thiolase-like.
DR InterPro; IPR041464; TubC_N.
DR InterPro; IPR044894; TubC_N_sf.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF18563; TubC_N; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 4.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF55048; Probable ACP-binding domain of malonyl-CoA ACP transacylase; 1.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Antibiotic biosynthesis {ECO:0000256|ARBA:ARBA00023194};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 37..460
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 941..1015
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2017..2092
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT REGION 1987..2023
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2093..2120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2627 AA; 291920 MW; 93FD8F2D8830BE16 CRC64;
MKRVPTELTD TGRVIKEALM EIRRLKRQLD EQRLIAREPV AVIGMACRFP GGITGPESFW
KVLMEMRDMI GEVPAHRWQS RAASASADSP YLRKAGFLTE DIEAFDHRLF QFSPREAERT
DPQQRLFLKV VWEALENSGY APNTLKGSKT GIYAGISLPD YMYALHLDRQ TSGTTEPNDV
AGSGFSFLSG RAAYFFGFQG PGITVDTACS SSLVAVDQAC KGLMAGDCEM AVAGGVNLMY
SPQTTELLSA LGILSSTCQM RSFDAGANGT VRGEGCGAVI LKRLSAAVRD GDSIHAVIRG
SGVNQDGLSS GLTAPYGPAQ EALLADVWER CGLDSHDLGY IEAHGTATAL GDPIELSALG
NVVAKDRESR LYVGTVKANI GHLEAAAGIA GLIKAIMAVE RGRIPGNPHF ETPSPHIEWE
RLPLDVPKET IAWESGGKPR AAGVSSFGLS GTNAHVVVEQ YRGERQDDRE PGARDNGGKR
WPFKFSSVTE DGLREQLAVF LEALERQGRD AAPGLPDLAY SQNISKADLK IRLVVWAGSR
EELAAAINRA LAGTPHASVS RGVRDKKVVF LFTGQGSQYP AMFTELYRDN PIFREGMDRC
SAVYREITGH DVMEIIASTG HDLNETRYTQ PALFAVEYSL ARMWMAYGVE PACMIGHSVG
EYAAACIAGV FEPEDAMRLI TARGELMHRL AERGKMAAVF AGRERVRRLL GSRTRVAVAA
ANTPGQTVVS GAAEEVDEVC RELNGEGVRT VPLQVSHAFH SPLMAPMLAE FKAIARTVKY
NAPKKAIISS ATGRPIDSEM ASPSYWTWQI QEEVKFLDCI RSLDDVADYV FLEVGPSPVL
TSMVEDICGG RTDCAASHIP QRDAAEQIER SFVHLYGRGV PVKWRALYAH ANLRKIAVPN
YRFSERRFGL DGPQEHSRPV EEKRSIVLAA ASSGPLPLTP EERKAYIRQA LIRELKLEED
ELADERNLLL HGLNSIVAAR LAAQWGNELG IRLNPGRLLG QCTIAQWADM LGEQTEQSAG
AEPETAAAFR MRPEQRGEPF QLNEVQLAYW AGRNAELEWG GVGCYAYFEI DAGGLDPVRF
KQALVALVRR HEMLRAEISA DGMQRIMPDI ELPLAVYRQE EIADLPAHLG LVRDEMSAQV
LPLGRPMFDL RLTEMGEDSW RVHFGIDFLI ADALSLHIFW SDLDRLYKGE PLPELKASFK
DYLQYVSERK QSSQIRRDRA YWLGKAEGFP SAPELPVNLS QATLDRRKFV RRQQWLSPEA
WHAFARAAAE RRLTPSAALL ALYAEVLSAW GGGGRFAVML TVFNREAVHP QIHEVIGDFT
QLALVDIRRE QTTAGRNADS VQRQMQADLA HVGYSAIDFV KELNNRDGAQ GRMYPVVFTS
ALGMEQLGGG SSTAFMNNLG WSVSSTPQVW LDHQVYAERD GVTLSWDTLD AVFQPGVVDA
MFAKYVELVE RAATEPGFWS ETLTDLRTDS QRRVHRRVNC TDNAYTGELL HGHIQCRAYT
DADRTAMICA DHSYSYGQLM ARADQVTELL QEQGVKPGDK VAIRMDKSFS QIAAVLGVVQ
AGAAYVPLAC DQPVGRMLDI VRRAGISILL ADRAEPAIGT EIAQFTAADW EGKQGIRQAV
DLDPAELAYV IYTSGSTGTP KGVCIAHGAA MNTIIDVNSR LGVTADDRIL GVSAYNFDLS
VYDIFGVLSA GGTLVLPSEE ERTDPKCWRR LSMQHGVTLW NSVPALLDLY TDYLLECGES
AVDGGIRHIL LSGDWIPLGL FEKAGKALPN AALTGMGGAT EASIWSNFYP IRGIDPDWTS
IPYGYPLANQ AYYILDEFGR PCPDGVKGQL HIAGKGLADG YLNEEALTSK VFYRHAELNE
RLYSTGDYGR YMKDGAIEFL GRMDNQLKIN GYRIEVGEIQ AAFAKCGVAG DVIVVPVGER
MESKKLVVYI KDDGATLPEP ELKQLLRGYL PGYSIPERMI AVPAFPMTAN GKIDRKALVR
SFIDIDGQNP SKAASDRAEQ PPERSSESPQ ELHSVFPEPP QELHPVLRTV REVLRMPELK
PADRLGDLGV SSVDMIRLAN RLEAEYADRP SVGEIIGHES VQELLDYYGE RAGKASEPQE
TPESLPQPIE PEERREDTEA ERLIERCRSL GIRLRAEDGR LTYKAAAGVM TPELQAELKS
CKQQLLDYIR ERGDEAEGAA WQSGSRAFRL TPIQLAYVLG RGADYELGGT SAHYYAEFEC
RHIDAYKLEQ AVNEVVRRHD MLRTVIYENG TQEVLAHTPV FRVPVRQIGD RRELEAIRSE
WSHHVYDLGE WPMFHVQISR LDDELSRLHF SFDCLIVDGW SAEMMFREIF KAYNGKPVYE
PEFTFRDYIR QEAGWLERKN YHKASADYWE RKLADTPPAP QLPFQTPLQN IAAPRFRRLK
LVLTEAQTRI LEERIRKHRF TPSAAVCTAY MKVLSHWSSR KDIALNLTLF NRLPLHPDVP
HMLGDFTNIA LISYEPEDGA SFVQETERIQ AQLWQAVENR THDGIGLLRR LARDAPGKAV
MPVVFTSLLF GESSAFEDDD FPPDMKEVFA ISQTPQVVID HQAYKRNGSM TLIWDYVEEA
FRLAEIEAMF RAYTELIERL IADGDDWRRE MAVSGEGYAG WREELKR
//
