NPS1_AJECA
ID NPS1_AJECA Reviewed; 1813 AA.
AC B2KWH8;
DT 20-JUN-2018, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 25-MAY-2022, entry version 62.
DE RecName: Full=Nonribosomal peptide synthase 1 {ECO:0000303|PubMed:18404210};
DE Short=NPRS 1 {ECO:0000303|PubMed:18404210};
DE EC=6.3.2.- {ECO:0000305|PubMed:18404210};
DE AltName: Full=Siderophore biosynthesis cluster protein NPS1 {ECO:0000303|PubMed:18404210};
DE AltName: Full=Siderophore synthetase NPS1 {ECO:0000305};
GN Name=NPS1 {ECO:0000303|PubMed:18404210};
OS Ajellomyces capsulatus (Darling's disease fungus) (Histoplasma capsulatum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Ajellomycetaceae; Histoplasma.
OX NCBI_TaxID=5037;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 26032 / G217B;
RX PubMed=18404210; DOI=10.1371/journal.ppat.1000044;
RA Hwang L.H., Mayfield J.A., Rine J., Sil A.;
RT "Histoplasma requires SID1, a member of an iron-regulated siderophore gene
RT cluster, for host colonization.";
RL PLoS Pathog. 4:E1000044-E1000044(2008).
RN [2]
RP INDUCTION.
RX PubMed=16030248; DOI=10.1091/mbc.e05-05-0434;
RA Nittler M.P., Hocking-Murray D., Foo C.K., Sil A.;
RT "Identification of Histoplasma capsulatum transcripts induced in response
RT to reactive nitrogen species.";
RL Mol. Biol. Cell 16:4792-4813(2005).
CC -!- FUNCTION: Nonribosomal peptide synthase; part of the gene cluster that
CC mediates the biosynthesis of hydroxamate-containing siderophores that
CC play a critical role in virulence via intracellular iron acquisition
CC during macrophage infection (PubMed:18404210).
CC {ECO:0000269|PubMed:18404210}.
CC -!- PATHWAY: Siderophore biosynthesis. {ECO:0000305|PubMed:18404210}.
CC -!- INDUCTION: Expression is induced during iron deprivation
CC (PubMed:18404210). Also induced in response to reactive nitrogen
CC species (PubMed:16030248). {ECO:0000269|PubMed:16030248,
CC ECO:0000269|PubMed:18404210}.
CC -!- DOMAIN: NRP synthetases are composed of discrete domains (adenylation
CC (A), thiolation (T) or peptidyl carrier protein (PCP) and condensation
CC (C) domains) which when grouped together are referred to as a single
CC module (By similarity). Each module is responsible for the recognition
CC (via the A domain) and incorporation of a single amino acid into the
CC growing peptide product (By similarity). Thus, an NRP synthetase is
CC generally composed of one or more modules and can terminate in a
CC thioesterase domain (TE) that releases the newly synthesized peptide
CC from the enzyme (By similarity). Occasionally, methyltransferase
CC domains (responsible for amino acid methylation) are present within the
CC NRP synthetase (By similarity). NPS1 has the following architecture: A-
CC T-C-T-C. {ECO:0000250|UniProtKB:A0A144KPJ6,
CC ECO:0000305|PubMed:18404210}.
CC -!- SIMILARITY: Belongs to the NRP synthetase family. {ECO:0000305}.
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DR EMBL; EU253973; ACC64451.1; -; Genomic_DNA.
DR AlphaFoldDB; B2KWH8; -.
DR SMR; B2KWH8; -.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 1.10.1200.10; -; 2.
DR Gene3D; 3.30.300.30; -; 1.
DR Gene3D; 3.30.559.10; -; 2.
DR Gene3D; 3.40.50.12780; -; 1.
DR InterPro; IPR010071; AA_adenyl_domain.
DR InterPro; IPR036736; ACP-like_sf.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR Pfam; PF00501; AMP-binding; 1.
DR Pfam; PF00668; Condensation; 2.
DR Pfam; PF00550; PP-binding; 2.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; SSF47336; 2.
DR TIGRFAMs; TIGR01733; AA-adenyl-dom; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 1.
PE 2: Evidence at transcript level;
KW Ligase; Multifunctional enzyme; Phosphopantetheine; Phosphoprotein; Repeat.
FT CHAIN 1..1813
FT /note="Nonribosomal peptide synthase 1"
FT /id="PRO_0000444383"
FT DOMAIN 624..699
FT /note="Carrier 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT DOMAIN 1282..1358
FT /note="Carrier 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT REGION 89..494
FT /note="Adenylation"
FT /evidence="ECO:0000255"
FT REGION 738..1159
FT /note="Condensation 1"
FT /evidence="ECO:0000255"
FT REGION 1427..1806
FT /note="Condensation 2"
FT /evidence="ECO:0000255"
FT MOD_RES 660
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
FT MOD_RES 1319
FT /note="O-(pantetheine 4'-phosphoryl)serine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00258"
SQ SEQUENCE 1813 AA; 199890 MW; 7A06708F93BEB6A7 CRC64;
MQLPFYVEAL ASNPKLLMKQ HGQHATLSLH AVHIQCSGFM DILDSILKNT DQTIGQAMQL
GDRELQQLWK WNASVPQTLD DCIHDIFVEK ARRDPSRQAV VSWDGELSYG EVDQFSTLLA
IHLIKLGVKF GNHVLLCFEK SMWTVVAVLA VMKSGGTLVL TDPSQPEARL QTIATEVGAN
LMLTSERQEE LGKRILAGGV IVVNHDFFQQ IQTSVLPPAS TTDLPSVPGS SPLYTIFTSG
STGKPKGVVI SHANYTSGAL PRAEAVGYGP HSRVLDFPSY AFDVSIDCML CTLAHGGCVC
VPSEDDRVNN LSGAIRNMKV NMAHMTPSVA RVLGEDTLSS LEVLGLGGES VSVRDAANWG
KLTKVIIAYG PSECTVGCTI NNEIALDRAY TSIGKGVGGV TWVVDPTDHS RLMPIGAIGE
LIIEGPIVGR GYLNDPERTS SVFIEDPMWL LSGCQGYPGR HGRFYKTGDL VKYDPDSSGS
IVFVGRGDQQ VKLRGQRVEL GEVEHHLRTR LPAGNVVAAE VITPGGKGDQ PTLVAFIAEK
TTTKSQTNKE IATFSTELRH SLEVMDKALG SVLPRYMVPS AYIPLLEMPL LVSCKVDRKK
LRSLGSAMSR KELIRHKTFS SQKEPQSERE RQLAHLWKCL FGAEAEIDVQ SNFFDLGGDS
LMAMKLVAAA RAENLLTSVA DIFRHPTLAE LAITLKHSDS EAEIDVPPFS LLDSHWKENN
ARIETAKLCG IDATSVMDVY PCTTLQEGLM ALSAKVSEAY VAQRVVELAD FQTAQRLQRA
FETAAADSPI LRTRIVQVPG RGLMQVVLKD GITWRAGTTL EEYLVKDRNE SMGLGTPLAR
FAITSNETTG KVHFVLTIHH ALYDGWSMPL VVRRVNRAFN NQESERSVAF NSFIKHLSGL
NHKDSEIYWK EQLQGANGLQ FPALPRAGYQ TQAQSLLEQY FPLGKTSASS TSIATSIRAA
WALVAGKYTL SDDVVFGETL TGRNAPVVGI EKIEGPMITT VPVRVRFDRN ARVSEYLRRI
HDDSILRIPH EHMGLQHIRR LSPDAREACE LRTGIVIHPT TTEDGKNLTG DGPANGFVPA
GDEDAAREAL KFNTYALMLV CSLDPKGFLV MASFDSATID VCQMDKVLGQ FGQTVQQLCE
NGNALVSDLL PMTDDELAEI WRFSNTYKPN SGNEVVLGHD YSHATATWIV APEDSEQLVP
LGGIGELVIE GDFPTNTSIQ ISGTKWLSAG HRDIPGRQAT LHKTGQLAKY NSDGSLVILG
GKGGNIKSDM EIKKPEAKSR SQVTTPKQQK LRKLWARVLG ISEDEVGSND SFFDLGGDSI
SAMKLVSEGR MENLELVVMQ VFQHRRFHDM ADIAKESLPL QVSTKQYSPF STLDVSDVDT
FISESIRPSL LNSSWKVVDV LPARPLQEIA VDGTINLPRY SARYELFYLD AAVDQSHLLK
SCQELISRNE ILRTIFVKSG GSCFGVVIEE LQLPLDEYQI DGDLTAFAEQ LCGLDIQTVM
SLGSPFIKFF VVQSSSGLSC LIMRISHAQY DEICLPILLR QLSALYEGEL VPAGLPFSSF
VHHIVRNNIP QSIEYWRRLL QGSSMSVLRP STPLISKKSI FISKTFDISS RSKEITLATL
PTAAWALCLA RRLSLRDVTF GEVVSGRNID FANCDTVVGP TWQYIPVRVK FKSGWTVIDL
LNFVQHQHIS STPFEGIGLK EIVRKCTDWP ETTEWFDSVV HQDVEHVESL RFLSANSRMD
TIYPHLEPLR EWKIQAFPKG DSLCIEIVTF ESWRAEADSI LNEMGDIISL LVTKPNSTLF
QTDVMEESTP PTS
