ID   OTC2_ECOLI              Reviewed;         334 AA.
AC   P06960; P78308; Q2MCE9;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 4.
DT   04-NOV-2026, entry version 194.
DE   RecName: Full=Ornithine carbamoyltransferase subunit F {ECO:0000303|PubMed:789338};
DE            Short=OTCase-2 {ECO:0000303|PubMed:789338};
DE            EC=2.1.3.3 {ECO:0000255|HAMAP-Rule:MF_01109};
GN   Name=argF {ECO:0000303|PubMed:789338};
GN   OrderedLocusNames=b0273, JW0266;
OS   Escherichia coli (strain K12).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6382166; DOI=10.1093/nar/12.15.6277;
RA   van Vliet F., Cunin R., Jacobs A., Piette J., Gigot D., Lauwereys M.,
RA   Pierard A., Glansdorff N.;
RT   "Evolutionary divergence of genes for ornithine and aspartate carbamoyl-
RT   transferases -- complete sequence and mode of regulation of the Escherichia
RT   coli argF gene; comparison of argF with argI and pyrB.";
RL   Nucleic Acids Res. 12:6277-6289(1984).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RA   Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA   Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA   Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT   "Sequence of minutes 4-25 of Escherichia coli.";
RL   Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-41.
RX   PubMed=3968036; DOI=10.1128/jb.161.2.714-719.1985;
RA   Falmagne P., Portetelle D., Stalon V.;
RT   "Immunological and structural relatedness of catabolic ornithine
RT   carbamoyltransferases and the anabolic enzymes of enterobacteria.";
RL   J. Bacteriol. 161:714-719(1985).
RN   [6]
RP   SUBUNIT.
RX   PubMed=4558857; DOI=10.1111/j.1432-1033.1972.tb01814.x;
RA   Legrain C., Halleux P., Stalon V., Glansdorff N.;
RT   "The dual genetic control of ornithine carbamolytransferase in Escherichia
RT   coli. A case of bacterial hybrid enzymes.";
RL   Eur. J. Biochem. 27:93-102(1972).
RN   [7]
RP   FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX   PubMed=789338; DOI=10.1128/jb.128.1.35-38.1976;
RA   Legrain C., Stalon V., Glansdorff N.;
RT   "Escherichia coli ornithine carbamolytransferase isoenzymes: evolutionary
RT   significance and the isolation of lambdaargF and lambdaargI transducing
RT   bacteriophages.";
RL   J. Bacteriol. 128:35-38(1976).
CC   -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from
CC       carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to
CC       produce L-citrulline, which is a substrate for argininosuccinate
CC       synthetase, the enzyme involved in the final step in arginine
CC       biosynthesis. {ECO:0000269|PubMed:789338}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=carbamoyl phosphate + L-ornithine = L-citrulline + phosphate +
CC         H(+); Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01109};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.02 mM for carbamoyl phosphate {ECO:0000269|PubMed:789338};
CC         KM=5 mM for L-ornithine {ECO:0000269|PubMed:789338};
CC   -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC       from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000305}.
CC   -!- SUBUNIT: In E.coli strain K12, trimer of identical or non-identical
CC       chains are composed of ArgI (I) and/or ArgF (F). The trimer has the
CC       following composition: FFI, FFF, FII, III. E.coli strains B and W,
CC       which are known to contain only ArgI, produce only a trimer of
CC       identical chains (III). {ECO:0000269|PubMed:4558857,
CC       ECO:0000269|PubMed:789338}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- MISCELLANEOUS: ArgF might be the product of a relatively recent event
CC       (duplication or transposition) peculiar to E.coli strain K-12.
CC       {ECO:0000305|PubMed:4558857}.
CC   -!- SIMILARITY: Belongs to the aspartate/ornithine carbamoyltransferase
CC       superfamily. OTCase family. {ECO:0000305}.
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DR   EMBL; X00759; CAA25329.1; -; Genomic_DNA.
DR   EMBL; U70214; AAB08694.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73376.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAE76057.1; -; Genomic_DNA.
DR   PIR; A64753; OWECF.
DR   RefSeq; NP_414807.1; NC_000913.3.
DR   RefSeq; WP_001281825.1; NZ_CP009789.1.
DR   SMR; P06960; -.
DR   BioGRID; 4261491; 21.
DR   ComplexPortal; CPX-5625; Ornithine transcarbamoylase complex, argFII variant.
DR   ComplexPortal; CPX-5626; Ornithine transcarbamoylase complex, argFFI variant.
DR   ComplexPortal; CPX-5627; Ornithine transcarbamoylase complex, argFFF variant.
DR   IntAct; P06960; 7.
DR   STRING; 511145.b0273; -.
DR   PaxDb; 511145-b0273; -.
DR   EnsemblBacteria; AAC73376; AAC73376; b0273.
DR   GeneID; 944844; -.
DR   KEGG; ecj:JW0266; -.
DR   KEGG; eco:b0273; -.
DR   KEGG; ecoc:C3026_01325; -.
DR   PATRIC; fig|1411691.4.peg.2007; -.
DR   EchoBASE; EB0065; -.
DR   eggNOG; COG0078; Bacteria.
DR   HOGENOM; CLU_043846_3_1_6; -.
DR   InParanoid; P06960; -.
DR   OMA; ADHHPCQ; -.
DR   OrthoDB; 9802587at2; -.
DR   PhylomeDB; P06960; -.
DR   BioCyc; EcoCyc:CHAINF-MONOMER; -.
DR   BioCyc; MetaCyc:CHAINF-MONOMER; -.
DR   SABIO-RK; P06960; -.
DR   UniPathway; UPA00068; UER00112.
DR   PRO; PR:P06960; -.
DR   AbasyAtlas; P06960; -.
DR   FunFam; 3.40.50.1370:FF:000004; Ornithine carbamoyltransferase; 1.
DR   Gene3D; 3.40.50.1370; Aspartate/ornithine carbamoyltransferase; 2.
DR   HAMAP; MF_01109; OTCase; 1.
DR   InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd.
DR   InterPro; IPR006130; Asp/Orn_carbamoylTrfase.
DR   InterPro; IPR036901; Asp/Orn_carbamoylTrfase_sf.
DR   InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd.
DR   InterPro; IPR002292; Orn/put_carbamltrans.
DR   InterPro; IPR024904; OTCase_ArgI.
DR   PANTHER; PTHR45753:SF4; ORNITHINE CARBAMOYLTRANSFERASE SUBUNIT F-RELATED; 1.
DR   PANTHER; PTHR45753; ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL; 1.
DR   Pfam; PF00185; OTCace; 1.
DR   Pfam; PF02729; OTCace_N; 1.
DR   PRINTS; PR00100; AOTCASE.
DR   PRINTS; PR00102; OTCASE.
DR   SUPFAM; SSF53671; Aspartate/ornithine carbamoyltransferase; 1.
DR   NCBIfam; TIGR00658; orni_carb_tr; 1.
DR   NCBIfam; NF009213; PRK12562.1; 1.
DR   PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004585; F:ornithine carbamoyltransferase activity; IDA:EcoCyc.
DR   GO; GO:0006974; P:DNA damage response; IEP:EcoliWiki.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IBA:GO_Central.
DR   GO; GO:0019240; P:L-citrulline biosynthetic process; IDA:ComplexPortal.
DR   Proteomes; UP000000625; Chromosome.
DR   AlphaFoldDB; P06960; -.
DR   FunCoup; P06960; 603.
PE   1: Evidence at protein level;
KW   Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW   Direct protein sequencing; Metal-binding; Reference proteome; Transferase;
KW   Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:3968036"
FT   CHAIN           2..334
FT                   /note="Ornithine carbamoyltransferase subunit F"
FT                   /id="PRO_0000112919"
FT   BINDING         56..59
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         83
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         107
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         134..137
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         168
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         232
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         236..237
FT                   /ligand="L-ornithine"
FT                   /ligand_id="ChEBI:CHEBI:46911"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         274..275
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   BINDING         320
FT                   /ligand="carbamoyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58228"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01109"
FT   CONFLICT        121
FT                   /note="A -> P (in Ref. 1; CAA25329)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   334 AA;  36827 MW;  C1EA07CD2AFC39C4 CRC64;
     MSDLYKKHFL KLLDFTPAQF TSLLTLAAQL KADKKNGKEV QKLTGKNIAL IFEKDSTRTR
     CSFEVAAFDQ GARVTYLGPS GSQIGHKESI KDTARVLGRM YDGIQYRGHG QEVVETLAQY
     AGVPVWNGLT NEFHPTQLLA DLMTMQEHLP GKAFNEMTLV YAGDARNNMG NSMLEAAALT
     GLDLRLLAPK ACWPEESLVA ECSALAEKHG GKITLTEDVA AGVKGADFIY TDVWVSMGEA
     KEKWAERIAL LRGYQVNAQM MALTDNPNVK FLHCLPAFHD DQTTLGKQMA KEFDLHGGME
     VTDEVFESAA SIVFDQAENR MHTIKAVMMA TLGE
//