ID A0A0W0WN86_9GAMM Unreviewed; 1593 AA.
AC A0A0W0WN86;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Peptide synthetase, non-ribosomal {ECO:0000313|EMBL:KTD33801.1};
GN ORFNames=Lnau_2093 {ECO:0000313|EMBL:KTD33801.1};
OS Legionella nautarum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC Legionellaceae; Legionella.
OX NCBI_TaxID=45070 {ECO:0000313|EMBL:KTD33801.1, ECO:0000313|Proteomes:UP000054725};
RN [1] {ECO:0000313|EMBL:KTD33801.1, ECO:0000313|Proteomes:UP000054725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49506 {ECO:0000313|EMBL:KTD33801.1,
RC ECO:0000313|Proteomes:UP000054725};
RA Burstein D., Amaro F., Zusman T., Lifshitz Z., Cohen O., Gilbert J.A.,
RA Pupko T., Shuman H.A., Segal G.;
RT "Genomic analysis of 38 Legionella species identifies large and diverse
RT effector repertoires.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KTD33801.1}.
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DR EMBL; LNYO01000021; KTD33801.1; -; Genomic_DNA.
DR RefSeq; WP_058505107.1; NZ_LNYO01000021.1.
DR STRING; 45070.Lnau_2093; -.
DR PATRIC; fig|45070.6.peg.2207; -.
DR OrthoDB; 9757559at2; -.
DR Proteomes; UP000054725; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0017000; P:antibiotic biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901566; P:organonitrogen compound biosynthetic process; IEA:UniProt.
DR CDD; cd12117; A_NRPS_Srf_like; 1.
DR CDD; cd08700; FMT_C_OzmH_like; 1.
DR CDD; cd05235; SDR_e1; 1.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.40.50.12230; -; 1.
DR Gene3D; 3.40.50.980; -; 2.
DR Gene3D; 1.10.1200.10; ACP-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; 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; IPR013120; Far_NAD-bd.
DR InterPro; IPR005793; Formyl_trans_C.
DR InterPro; IPR002376; Formyl_transf_N.
DR InterPro; IPR036477; Formyl_transf_N_sf.
DR InterPro; IPR011034; Formyl_transferase-like_C_sf.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR010080; Thioester_reductase-like_dom.
DR NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR NCBIfam; TIGR01746; Thioester-redct; 1.
DR PANTHER; PTHR44845:SF6; BETA-ALANINE-ACTIVATING ENZYME; 1.
DR PANTHER; PTHR44845; CARRIER DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF13193; AMP-binding_C; 1.
DR Pfam; PF02911; Formyl_trans_C; 1.
DR Pfam; PF00551; Formyl_trans_N; 1.
DR Pfam; PF07993; NAD_binding_4; 1.
DR Pfam; PF00550; PP-binding; 1.
DR PRINTS; PR00154; AMPBINDING.
DR SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR SUPFAM; SSF47336; ACP-like; 1.
DR SUPFAM; SSF50486; FMT C-terminal domain-like; 1.
DR SUPFAM; SSF53328; Formyltransferase; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00455; AMP_BINDING; 1.
DR PROSITE; PS50075; CARRIER; 1.
PE 4: Predicted;
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000054725}.
FT DOMAIN 1091..1166
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 1593 AA; 180957 MW; 5AFF78C3D5F876C3 CRC64;
MEKKLVTCYL IGEDRLLLEC AEILLSYNHS ILGIISPLPA AEEFSIQKKI PYFLKVSDAV
PILSVTAFDY LFSIINGTVL PLSLLEQAKC MAINYHNGPL PRYAGLHAPS WAILHNERVH
GVTWHQMVKD IDAGAILKQA PIEIEADETG LSLSVKCYQE ALNTFKELVY EISFQQLRPI
PQNLENRSYF DYCQKPMNGG WISWHDSAET IDRMCRALNL GQHHRNRFSL PKFNIGKNFF
LILQLHILDE ENSHAPGTLV EITAQYWQIA TKTRVVQLEQ ILSFHNETVD FIELAERFHL
KKGSVLPPIS EKSRLEYKYF CEVYAIHELF WVRQEKSFIP ATLPFQTLSL SPEKNYPLKQ
VAMFNASTLF SFPTNEYPNN PCNILFAALY IYLYRLGNKE KFGVGFSHPL LQQLPEAIKP
LFAQIIPFSF QLNEDLTVEE TLKEFFDRLL KFDKHLSFSR DIFVRYPELS SNLQSFYPIT
VMIGHEKGFL KRIHHINSSV VVTISNTYKI QWFSREKNDD LDTILRNSIQ HLPILIASML
EHPTMLISQL PLLSAKESSQ LLMTWNKTQI SPSQNKSVVQ LFVEQVQKTP EQIALSYEGQ
VLSYQALNDQ SNQFARLLQK NGLSAGQHVV ICTNQEIHLI VGLLAILKIG AAYVPIDTNY
PSSHIQFILS DSSATVAIAS KSLKAKMQIC CDNQNVPLII FENFIKSASA ESSENLNLAS
VDPDSLAYII YTSGTTGKPK GVMIPHRGIV RLVNSTNYIK ITKNDRIAQA ASISFDAATF
EIWGALLNGA TLVAVPHATL VNVTQFSQFL IKKKITVLWL TSALFNQYAS VKPSMFATLS
YLLIGGDILN AEQVMRVLRC EKGAPRQILN GYGPTENTTF TTTYLIKARK EGYQSIPIGK
PIANSTVYIL DKYLRPTPIG APGELYTGGA GVALGYLNRP EITTARFIPN LFDSSAETLL
YKTGDIVRWM PDGNIEYLSR QDNQIKIRGF RVELEAVCTV LLHHEAVDQC AVRVCENEKQ
QKSIVAYLVL KHECPMINIK QYMASQLPKY MIPSFFIRID KIPLTLNGKV DFEKLPAPDS
STNTLTSEYV APQTQTEKEI EKIWSELFEL DQIGIHDSFF DLGGHSLMVS QLVLKVKEQL
LYDLSLQQFL EKPTIFHLAQ LIEINEEIKP SSFMAHWKFD IELNLPHCLR VTKPNIFSDF
PSKREREPNF LQELEAANVQ PKALLLTGAN GFLGANLLKQ LYQLTSATIY CLVRGANLED
AKNKLQKSIE LYDLHFEDKE RIQLLVGDLG KPYLGLPIEE FMVLAEKIDI IYHNGAAVHH
LYSYEMLRAA NVLSVKEILK LATIKKLIPI HYISTLSAAS NYLDNFNSII EDFIYSHPNP
PPEDGYSQTK WIAEQILAKA HQQQIPIKIY RPAWILGDSI SGLIAAEQNH LLRLIKGCCQ
LGYAPSWDIE LDILPVDYVG QMIVKTSLNT KIPYSLFNLV NTNKLSWKEL ITYLNQRGYN
MQLISPNAWQ KKLLTEMSPE STLYSLLTLY INQSDNVWME KLDRISSANN QNTHYAFQAN
GMKFPFINKQ LLDNYFNFLE KRGFLAIKVA DVI
//