ID B4EXX8_PROMH Unreviewed; 3071 AA.
AC B4EXX8;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 113.
DE SubName: Full=Non-ribosomal peptide synthase (Putative siderophore synthase) {ECO:0000313|EMBL:CAR45150.1};
GN Name=nrpS {ECO:0000313|EMBL:CAR45150.1};
GN OrderedLocusNames=PMI2600 {ECO:0000313|EMBL:CAR45150.1};
OS Proteus mirabilis (strain HI4320).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Proteus.
OX NCBI_TaxID=529507 {ECO:0000313|EMBL:CAR45150.1, ECO:0000313|Proteomes:UP000008319};
RN [1] {ECO:0000313|EMBL:CAR45150.1, ECO:0000313|Proteomes:UP000008319}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HI4320 {ECO:0000313|EMBL:CAR45150.1,
RC ECO:0000313|Proteomes:UP000008319};
RX PubMed=18375554; DOI=10.1128/JB.01981-07;
RA Pearson M.M., Sebaihia M., Churcher C., Quail M.A., Seshasayee A.S.,
RA Luscombe N.M., Abdellah Z., Arrosmith C., Atkin B., Chillingworth T.,
RA Hauser H., Jagels K., Moule S., Mungall K., Norbertczak H.,
RA Rabbinowitsch E., Walker D., Whithead S., Thomson N.R., Rather P.N.,
RA Parkhill J., Mobley H.L.;
RT "Complete genome sequence of uropathogenic Proteus mirabilis, a master of
RT both adherence and motility.";
RL J. Bacteriol. 190:4027-4037(2008).
CC -!- COFACTOR:
CC Name=pantetheine 4'-phosphate; Xref=ChEBI:CHEBI:47942;
CC Evidence={ECO:0000256|ARBA:ARBA00001957};
CC -!- PATHWAY: Lipid metabolism; fatty acid biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005194}.
CC -!- SIMILARITY: Belongs to the thiolase-like superfamily. Beta-ketoacyl-ACP
CC synthases family. {ECO:0000256|ARBA:ARBA00008467}.
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DR EMBL; AM942759; CAR45150.1; -; Genomic_DNA.
DR RefSeq; WP_012368440.1; NC_010554.1.
DR ESTHER; promi-NRPS; Thioesterase.
DR EnsemblBacteria; CAR45150; CAR45150; PMI2600.
DR GeneID; 6801278; -.
DR KEGG; pmr:PMI2600; -.
DR PATRIC; fig|529507.6.peg.2536; -.
DR eggNOG; COG1020; Bacteria.
DR eggNOG; COG1028; Bacteria.
DR eggNOG; COG2226; Bacteria.
DR eggNOG; COG3319; Bacteria.
DR eggNOG; COG3321; Bacteria.
DR HOGENOM; CLU_000022_33_1_6; -.
DR UniPathway; UPA00094; -.
DR Proteomes; UP000008319; Chromosome.
DR GO; GO:0004315; F:3-oxoacyl-[acyl-carrier-protein] synthase activity; IEA:InterPro.
DR GO; GO:0031177; F:phosphopantetheine binding; IEA:InterPro.
DR GO; GO:0006633; P:fatty acid biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0018130; P:heterocycle biosynthetic process; IEA:UniProt.
DR GO; GO:1901362; P:organic cyclic compound biosynthetic process; IEA:UniProt.
DR GO; GO:0009403; P:toxin biosynthetic process; IEA:UniProt.
DR CDD; cd02440; AdoMet_MTases; 1.
DR CDD; cd19535; Cyc_NRPS; 1.
DR CDD; cd05274; KR_FAS_SDR_x; 1.
DR CDD; cd00833; PKS; 1.
DR Gene3D; 3.30.70.3290; -; 1.
DR Gene3D; 3.40.47.10; -; 1.
DR Gene3D; 1.10.1200.10; ACP-like; 2.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 3.40.366.10; Malonyl-Coenzyme A Acyl Carrier Protein, domain 2; 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 Gene3D; 3.40.50.150; Vaccinia Virus protein VP39; 2.
DR InterPro; IPR029058; AB_hydrolase.
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; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR001242; Condensatn.
DR InterPro; IPR018201; Ketoacyl_synth_AS.
DR InterPro; IPR014031; Ketoacyl_synth_C.
DR InterPro; IPR014030; Ketoacyl_synth_N.
DR InterPro; IPR013217; Methyltransf_12.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR InterPro; IPR032821; PKS_assoc.
DR InterPro; IPR020841; PKS_Beta-ketoAc_synthase_dom.
DR InterPro; IPR013968; PKS_KR.
DR InterPro; IPR020806; PKS_PP-bd.
DR InterPro; IPR009081; PP-bd_ACP.
DR InterPro; IPR006162; Ppantetheine_attach_site.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR InterPro; IPR001031; Thioesterase.
DR InterPro; IPR016039; Thiolase-like.
DR PANTHER; PTHR43775; FATTY ACID SYNTHASE; 1.
DR PANTHER; PTHR43775:SF37; FATTY ACID SYNTHASE; 1.
DR Pfam; PF00698; Acyl_transf_1; 1.
DR Pfam; PF00668; Condensation; 1.
DR Pfam; PF16197; KAsynt_C_assoc; 1.
DR Pfam; PF00109; ketoacyl-synt; 1.
DR Pfam; PF02801; Ketoacyl-synt_C; 1.
DR Pfam; PF08659; KR; 1.
DR Pfam; PF08242; Methyltransf_12; 2.
DR Pfam; PF00550; PP-binding; 2.
DR Pfam; PF00975; Thioesterase; 1.
DR SMART; SM00827; PKS_AT; 1.
DR SMART; SM00822; PKS_KR; 1.
DR SMART; SM00825; PKS_KS; 1.
DR SMART; SM00823; PKS_PP; 2.
DR SUPFAM; SSF47336; ACP-like; 2.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 2.
DR SUPFAM; SSF52151; FabD/lysophospholipase-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 2.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 2.
DR SUPFAM; SSF53901; Thiolase-like; 1.
DR PROSITE; PS50075; CARRIER; 2.
DR PROSITE; PS00606; KS3_1; 1.
DR PROSITE; PS52004; KS3_2; 1.
DR PROSITE; PS00012; PHOSPHOPANTETHEINE; 2.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315};
KW Fatty acid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Fatty acid metabolism {ECO:0000256|ARBA:ARBA00022832};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00023160};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023160};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Phosphopantetheine {ECO:0000256|ARBA:ARBA00022450};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 11..435
FT /note="Ketosynthase family 3 (KS3)"
FT /evidence="ECO:0000259|PROSITE:PS52004"
FT DOMAIN 1742..1816
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
FT DOMAIN 2765..2838
FT /note="Carrier"
FT /evidence="ECO:0000259|PROSITE:PS50075"
SQ SEQUENCE 3071 AA; 345282 MW; 5EDCA59076C4ED3C CRC64;
MLNFETFYGN SEPIAVIGLS GRFPDAQNID QFWHNIINKH DSSRLFSEEE LKAAGVAEQT
YHSPDFVNRG APLDEAEYFD ATLFNYSRSE AELIDPQQRI FLQGAWHALE HAGYAPCNIT
IKTGVFASAR MSSYPAQQDL ALHNIGHVRG MQKLLGNDKD YLATRIAYKL NLTGPALTIQ
TACSSSLVAV HMACESLRSG ECSMAIAGGI GITFPQTGGY LYQKGMIFSP DGICRPFDAE
ANGTFAGNGF GIVVLRRLED ALVDGNTIIA VLRGSAINND GHQKAGFTAP SVAGQVSVIR
EAIQLADIKN EDIELIEAHA TATPLGDPIE FSALCQVFAD RSLTASKCAI GSVKGNIGHL
DTAAGITGLI KTILAVNKAL IPPSMHFNHP NPQLQIEKSP FYIPKNPKAW SSRIRTAGVS
SFGIGGTNCH IIVQSLPDSL VSIKPEQEVD NNFEYSLLLS AATKESLKKL AGDYAPLIKI
TPANILAHNA LQQRQLNLPW RLSIPLTSES DISLLAFSQG SADSLIQYGH TSTNKKIAWL
FSGMGSQYPA MGKVMYQHST TFAETIDRCE QACLQHLTFP LKEVMFGLHS DKLVNASYIQ
AAIVAYEIAM AAHWRAIGIL PEIIVGHSCG EYAAAVIAGF YTIEQMMPLA VYSGQLMESH
VNGEMIAVFA EYQDIQIIAK QCHVELAAIN GHNNLSFAGQ PDDMQKFTQI LKAKNIRFRE
MNNVCAAHTS YIDNILDQLM EFTESLSASQ GKIALVSGYT GQLISQKELQ HPSYWAQQLR
NTVMYQDAIQ TLVNHGVTHA MELGPTSVLS DLGEREGITE ISWIPTARMG VDEIQMKQQA
ATTLFIAGYD LPWQSLFKTQ GSYIPLPLYP FEKQYYWYEK KDSEKYQPQK SAFDLPISQG
RETALKALTT LDLPRLNSFN STLTTLHNYY VDKMICSCLG HELNTPMSVI DIMRAGRILP
RYYQLLVRLL EACVEDGYYI YQQINQHNYY KKIKSISSDK LPLLFHQLQL DSEGLQSIPD
TVKRAGEQLY DMMTGVIEPV SVIFPEGASQ GVEVLYQDFS FGRYFNQIAA AVLKGLLSHY
QPTVAKPLRI IEVGGGTGGT TSWLLPILST IQHVEYEFTD ISPIFTRRAA QKFSQYSFVN
YREFNLQQSP EIQGFQSDYY DIIIAANVIH ATQHIGDTLT ALRTLLRSNG HLLMREITKQ
ARLFDFVFGP LVLPLHDEKI RKGKLFLSPE LWHQQCRLAG FQHIRWLPDA LPETKDMCEH
IILASVSTEN DHFDQELPSD TKIQQSSHYQ WQLTPCVEQD LIKPTLIFNH QQTLPSEITA
ILSAIGCLSE QGENQLIVAN LADPLIIAEQ IRQILLSSSD GFVVITQQAW ALTAIETVNP
AQRSIRSLLK TIQKEYSSRL IAIVDLGINA SWSELVPAFI QIEQGNNEII VRNHCCYLPQ
LTPLPSSSTI IAQNIMVSPR WHIITGGFGG LGRITASWLV RQGAKRIAIL APRADSSALD
WMNNLQKSNQ LEIKWLTCDC RDNAKCHAAL TQLENEGGIE GLIHSAGILD DALMTQLTPK
RMSDVFSVKA ISAKQFCDAL EKTDASYLIL YSSAAATIGS EGQAAHSLAC GYLDGLAEYA
RRNIKGLTVI SIAWGAWQSV GFVAEKQLHD KLQHKGMSTL TTEEGLAHLD ACLLDNTSCR
LAMRLATPPL MTQKTPLFHQ TNHNDHYDNH EINHTRQLCE TPTQTDQTEP VSPNRVDYRV
GDNLEQWLTA CIKQLLRLGD EHIDTHIELF QLGLDSLSFL DLSAEIKKQF AVNIDAEQSY
DDMTIAGLAS VIRTAAPEKF TVTEALHNQD NISHTMESER YAPFPLTPIQ HAYWIGRKNL
FNYGGVACHA IFEWDCQRHI WEPASLEKAW NKVIQRHDML RMIIDDDGQQ RILKEVPYFH
FIQHDLTNLT QQEQQESLTQ IREALSYRVL PTESWPLFEV EISWLNNDCY RLHINLDLLQ
FDTMSFKILF DDLFNAYSGQ ELIPQTFTFR DYCLKNQTNR NSDEWKMAWC YWQDLLSDLP
SAPYLPIKNS SITEQPRFTT FQHHVSIAQW DKLKQRWKKH GITPSAGLLT LFALVLGRWT
KYPAFTLNLT FFNRQPWHPD VTQLIGDFTS VLPIDIYLDN DCTLNESMAK IQRRLWQHLS
KSQVNGVEIL REWGRYKGDS SQSLLPIVFT SMLGMTLDGD NIDEALNQLF GQPVYSFAQT
PQVWLDHQVM EGKEGLTLNW FCMDDIFADG LLTMMFSDYQ SLITQLCQDE DNNQSVDKII
AQLPSYQHLA IDNHLQSRYQ QLEQTLENHP QIKRAHAMVM VKDDTKVEPP LQLLFEASSD
IPLSVIKQPN WLPNLLSPSA SLSDIIEKSW QRFEERARYG ICHTLYRNAL FTELNTPITL
AEIVARLKAK PQYERLLSQW LDLLCLHHLL TKEGDQFYAT TQFINLCLSA PVFQQPVNDW
EYVLWDYLEQ SLTQHELLFS GKVSPLSLLF NSDEITTALY AKHPALNYLN QCAKDIVSAM
VGATSSLNIL EIGAGTGATT QGIVAVLKNT HYSYTFTDIS HYFLDKARKK FTAVGEMRYQ
LFDINAPIQF SHHPDNGYDL IIASNVLHDA SHIGHALKRI RSLLKPQGYL LFIEATECQS
AMQMATVGFI EGLSAYQDKR ILTNKAMLDS ESWHDILINT GFETIGQWPQ TDSSSLRQTL
FLASPTRGGK PYLGKLRDYL SHSLDQNIDS FELFQCENIE ATLNGIATSS AQELNEQIQP
VAIPDVPTNM INEIIALWSE LLGREVNSTN DFFRSGGDSL IATKMISQLH QRGYPATLQQ
IFTYPCLADF CAHLEQEKQS QREYSSLIPL SAVSAPKPYH YFMVHASDGD PGVYLPLAES
LNNTVWGLTV TDASKLTDLD TLLSLHLSSI KTAQQTGPYI LIGWSYGAFI ASYLAEQLSQ
QNHSVLLVLI DPVYRHDFIK FCHDDSDSSS DENKQLACTK RLMSFLPESD LPLSDDIACL
WLEATNHPTE WTSPEKEWYQ RLPPHTQHHY FSGEHWSILQ DRATSTHLAE IIDQWVQQKL
SNNGYPSEGG N
//
