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Database: UniProt
Entry: A0A098G2Y5_9GAMM
LinkDB: A0A098G2Y5_9GAMM
Original site: A0A098G2Y5_9GAMM 
ID   A0A098G2Y5_9GAMM        Unreviewed;      1983 AA.
AC   A0A098G2Y5;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:CEG56818.1};
GN   ORFNames=LFA_1397 {ECO:0000313|EMBL:CEG56818.1};
OS   Legionella fallonii LLAP-10.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=1212491 {ECO:0000313|EMBL:CEG56818.1, ECO:0000313|Proteomes:UP000032430};
RN   [1] {ECO:0000313|Proteomes:UP000032430}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC700992 {ECO:0000313|Proteomes:UP000032430};
RA   Gomez-Valero L.;
RL   Submitted (SEP-2014) 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: Siderophore biosynthesis. {ECO:0000256|ARBA:ARBA00004924}.
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DR   EMBL; LN614827; CEG56818.1; -; Genomic_DNA.
DR   RefSeq; WP_045095426.1; NZ_LN614827.1.
DR   STRING; 1212491.LFA_1397; -.
DR   KEGG; lfa:LFA_1397; -.
DR   HOGENOM; CLU_234227_0_0_6; -.
DR   Proteomes; UP000032430; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR   GO; GO:0043604; P:amide biosynthetic process; IEA:UniProt.
DR   GO; GO:0019752; P:carboxylic acid metabolic 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   Gene3D; 3.30.300.30; -; 1.
DR   Gene3D; 3.40.50.980; -; 2.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 1.10.1200.10; ACP-like; 1.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR016181; Acyl_CoA_acyltransferase.
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; IPR010037; FkbH_domain.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR010033; HAD_SF_ppase_IIIC.
DR   InterPro; IPR020806; PKS_PP-bd.
DR   InterPro; IPR009081; PP-bd_ACP.
DR   InterPro; IPR006162; Ppantetheine_attach_site.
DR   InterPro; IPR001031; Thioesterase.
DR   NCBIfam; TIGR01733; AA-adenyl-dom; 1.
DR   NCBIfam; TIGR01686; FkbH; 1.
DR   NCBIfam; TIGR01681; HAD-SF-IIIC; 1.
DR   PANTHER; PTHR45527:SF1; FATTY ACID SYNTHASE; 1.
DR   PANTHER; PTHR45527; NONRIBOSOMAL PEPTIDE SYNTHETASE; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00501; AMP-binding; 1.
DR   Pfam; PF13193; AMP-binding_C; 1.
DR   Pfam; PF00668; Condensation; 1.
DR   Pfam; PF00550; PP-binding; 2.
DR   Pfam; PF00975; Thioesterase; 1.
DR   SMART; SM00823; PKS_PP; 1.
DR   SMART; SM01294; PKS_PP_betabranch; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 1.
DR   SUPFAM; SSF47336; ACP-like; 2.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   PROSITE; PS00455; AMP_BINDING; 1.
DR   PROSITE; PS50075; CARRIER; 2.
DR   PROSITE; PS51186; GNAT; 1.
DR   PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE   4: Predicted;
KW   Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032430}.
FT   DOMAIN          378..532
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          577..656
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
FT   DOMAIN          1642..1719
FT                   /note="Carrier"
FT                   /evidence="ECO:0000259|PROSITE:PS50075"
SQ   SEQUENCE   1983 AA;  227757 MW;  481B3ACBEFEFDE0A CRC64;
     MINITSTFTA DILRPSLQSI LKKFSEQKIQ FFYNQTFQQI LLPNSEFNQN EEGVNVILVR
     LSDLFNPLND SAQSPEELLT ALHRFNRTKR IPLLIIITPT EVKSQNDEQF YTKIENQIQL
     ESHAWKNTLL VTSKEMLKES NLSLIFDNFT EKHGHIPYSL DFYNLMGLTI ARKYSLLSRK
     PSKVIVLDCD GTLWNGIIEE DGINGIIIDE EYVAIQEFMI ELHHAGFLLC LCSKNSESSV
     LNVFKNHEDI VLDLEKHICG HRINWQPKSI NIQSLAQELN LGLDSFIFID DNNIECAEVK
     STIPEVFVIE LPKRSNSEKN SNFNRSHFLR NIWAFDYLEK SNEDEKRTEF YKQNKLRHQL
     KEKSFSYEQF IKNLKIKTCI REATTNDLQR VIQLSQRTNQ FNLLPNTISA VEFEHSIHNK
     KPHCLVIEVS DKYGEYGLVG VVAYDFHNNE LIINGFFLSC RILGRGIEFE IIKHLADTAS
     QNGISTIKLR FTKTEKNIPA INFIKQLNGQ NNQEPIDHII LSIDFIKEIS PEIFEQKNQS
     TIQNKKDSHQ TNISNGFMLE IANEHFQKSM NTKESKRNIT QGTDALEISI LEILKQHDLW
     TKKTDISFID LGIDSLKSVL IASDIYQRYQ IEITPFDLLK PNYTIDKFLK LLLKEIKQTE
     IKAPALNLIG YDTIPLSSAQ KRIWYDEKIS PESRKNNIFV AYEIKGNVSK EHLKKAFKQL
     MARHDALRFS FSEQENQPFI ILNPLESIDF KIDIFKNLAN QDFGNYLKKF KHQHFDLGAA
     PLFRVSLAHI EKDKTIFLFC IHHIIHDGWS LNILLHDLSQ LYNTLSKNIP LSITNQSSFL
     NFISWQRDNI SEELLTKQKD FWVKQLNKMP KLELIYDKAR KEGTEKQLSK RINFKISNTV
     TRQLKKISIN NQATLYDVLI TAFGLFLSHY SNQNDVNFIT AVSGRHHSHV AHVIGFFVNL
     LLIRLHLNPD ETFDALIRKN KKLLHDVFEN QDFPFNEMAQ LTGEQVNSKI HSFSQAGFIF
     QSYPINELVI NNEVCKRVYS DDHAELIYDS CDECRFGNLV CYMQEFNSEL HGIFEYNTLL
     FNKNTITHMI SAFKTLLKNI AVYQDRPALS IPLLTDTQIN TLFYKWNPPI INEPEHVTIL
     NYFAEQVSAH PNKIAVKHHE NTLTYEQLDK ISNQLAHKLQ KTMISPEMPI GIFLEKGINR
     IIAILGILKA GGCYVPLEID IPAARISYII NNASISIIIT SNELIPNIEE ISPSVTKISI
     TDNSIQAESD SPVDNNQFNP NQLTYILYTS GSTGTPKGVS VEQAGILRLV KNANYIKIKS
     SDRVAQTSSF LFDAATLEIW GALLNGATLV LIDKQTLLDE HLFSSILKNE EISILFLTTQ
     LFHAYAYTAP YLFQHLTYLA VGGEAVLSEA IERVFQQKKR PRYFINGYGP TENTTFSTTY
     VVKNQRDIVN PIPIGQPLTG TQVYVLGKDM NPKPIGAPGK LYLGGVGLAR GYINQPQLNQ
     EKFITHHNKR LYDTGDIVTW QTNGHLKFIG REDNQIKING YRIELNEIEA QLETHHLVEQ
     AIVLVKNKDH HHQLFAYVLL QEGNSLTDIN LYHYLKTFLP HYMIPNFYHQ IDTVPLTENG
     KADKKLLAKM DLHYTSYTEY ESAASLLQEK LISIYAEILR INPKNISINA EFFDIGGNSI
     SALNLISRIN DQFHVKINFS LLYEYATVKL LSEKISLLIS EAHFSSTVDH AKQYENALKI
     IKIGSNHKTP IVFIHPIGGT GFCYLDLIKL LPNDQPCYLI QDPSIDANQI LFDDIHSMAK
     YYNHLLLKQI KNSKFILAGY SFGGMLALEM TAQLEEKKLD DCIDFIISFD TWVVSDFMDI
     SAKEALKASI MNQYERVAKA LSNENIDPKP WMELYYCRLQ DLGFAYTPPK IKKRIMLFKA
     QQQAGEFSAM NDATNFLSLH SAKEIDVYLT PGNHDSILQF PNVRYISDTL HNYFADTLNE
     LDC
//
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