CTU_FRATT
ID CTU_FRATT Reviewed; 286 AA.
AC Q5NHL7; A0A0G2RPP9;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Citrullinase {ECO:0000305};
DE EC=3.5.1.20 {ECO:0000269|PubMed:19502406, ECO:0000269|Ref.3};
DE AltName: Full=Citrulline ureidase {ECO:0000303|PubMed:19502406};
DE Short=CTU {ECO:0000303|PubMed:19502406};
GN Name=ctu {ECO:0000303|PubMed:19502406};
GN OrderedLocusNames=FTT_0435 {ECO:0000312|EMBL:CAG45068.1};
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=19502406; DOI=10.1128/jb.00212-09;
RA Mahawar M., Kirimanjeswara G.S., Metzger D.W., Bakshi C.S.;
RT "Contribution of citrulline ureidase to Francisella tularensis strain Schu
RT S4 pathogenesis.";
RL J. Bacteriol. 191:4798-4806(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX DOI=10.1016/j.jab.2014.11.003;
RA Zhu T., Fang S., Wang W., Wang K., Cui Z., Wang C.;
RT "The expression, purification and activity analysis of Francisella
RT tularensis citrulline ureidase in Escherichia coli.";
RL J. Appl. Biomed. 13:189-194(2015).
CC -!- FUNCTION: Catalyzes the degradation of citrulline into ornithine,
CC carbon dioxide and ammonia (PubMed:19502406, Ref.3). Contributes to
CC intramacrophage survival, in vivo growth and pathogenesis
CC (PubMed:19502406). {ECO:0000269|PubMed:19502406, ECO:0000269|Ref.3}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + H2O + L-citrulline = CO2 + L-ornithine + NH4(+);
CC Xref=Rhea:RHEA:11940, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:28938, ChEBI:CHEBI:46911,
CC ChEBI:CHEBI:57743; EC=3.5.1.20;
CC Evidence={ECO:0000269|PubMed:19502406, ECO:0000269|Ref.3};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11941;
CC Evidence={ECO:0000305|PubMed:19502406};
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in loss of CTU
CC activity (PubMed:19502406). Loss of the gene does not affect acellular
CC growth, but it impairs intramacrophage survival in resting as well as
CC gamma interferon-stimulated macrophages (PubMed:19502406). Mice
CC infected intranasally with the mutant show significantly reduced
CC bacterial burden in the lungs, liver and spleen compared to wild-type
CC Schu S4-infected mice (PubMed:19502406). Mice infected with the mutant
CC succumb to infection, but they survive longer and show significantly
CC extended median time to death compared to that shown by wild-type Schu
CC S4-infected mice (PubMed:19502406). {ECO:0000269|PubMed:19502406}.
CC -!- BIOTECHNOLOGY: Is a good candidate for development of an efficient and
CC cost-effective enzymatic-based method for preparation of ornithine.
CC {ECO:0000269|Ref.3}.
CC -!- SIMILARITY: Belongs to the carbon-nitrogen hydrolase superfamily.
CC {ECO:0000305}.
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DR EMBL; AJ749949; CAG45068.1; -; Genomic_DNA.
DR RefSeq; WP_003020185.1; NZ_CP010290.1.
DR RefSeq; YP_169475.1; NC_006570.2.
DR IntAct; Q5NHL7; 5.
DR DNASU; 3191421; -.
DR EnsemblBacteria; CAG45068; CAG45068; FTT_0435.
DR KEGG; ftu:FTT_0435; -.
DR PATRIC; fig|177416.36.peg.422; -.
DR OMA; NAPYFCQ; -.
DR BRENDA; 3.5.1.20; 14771.
DR Proteomes; UP000001174; Chromosome.
DR GO; GO:0050126; F:N-carbamoylputrescine amidase activity; IEA:InterPro.
DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro.
DR Gene3D; 3.60.110.10; -; 1.
DR InterPro; IPR003010; C-N_Hydrolase.
DR InterPro; IPR036526; C-N_Hydrolase_sf.
DR InterPro; IPR017755; N-carbamoylputrescine_amidase.
DR Pfam; PF00795; CN_hydrolase; 1.
DR SUPFAM; SSF56317; SSF56317; 1.
DR TIGRFAMs; TIGR03381; agmatine_aguB; 1.
DR PROSITE; PS50263; CN_HYDROLASE; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Reference proteome; Virulence.
FT CHAIN 1..286
FT /note="Citrullinase"
FT /id="PRO_0000456187"
FT DOMAIN 4..258
FT /note="CN hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 43
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 116
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
FT ACT_SITE 153
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00054"
SQ SEQUENCE 286 AA; 32430 MW; D5C6AEF966556119 CRC64;
MANIKVAVVQ LSFNDNEAEN LAKLESKIIQ AAKNGAKIIL TPELPSYLYF CKKQNSKYFD
LAKTIDESPI VKLYKLLAHK YNIVLPASFF ERDGNACYNS IAMIDADGSI MGVYRKAHIP
DGIGYQEKYY FSPGSAGFKV WDTKYAKVGV GICWDQWFPE AARVMALKGA EILLYPTAIG
SEPHLPDYDS KDHWQRVMQG HAAANMLPVL ASNRYATEAN DDITATYYGS SFITDHTGDK
IAEADRSGDD ILYATFDFAE LQQQRFYWGL FRDRRPELYD EIVRKY
