PXPB_BACSU
ID PXPB_BACSU Reviewed; 240 AA.
AC P60495; P42967;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2004, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=5-oxoprolinase subunit B {ECO:0000305};
DE Short=5-OPase subunit B {ECO:0000305};
DE EC=3.5.2.9 {ECO:0000269|PubMed:28830929};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit B {ECO:0000305};
DE AltName: Full=Antikinase KipI {ECO:0000303|PubMed:18823995};
DE AltName: Full=Kinase A inhibitor;
DE AltName: Full=Sporulation inhibitor KipI;
GN Name=pxpB {ECO:0000303|PubMed:28830929};
GN Synonyms=kipI {ECO:0000303|PubMed:9334321}, ycsJ;
GN OrderedLocusNames=BSU04080;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8574415; DOI=10.1099/13500872-141-12-3241;
RA Akagawa E., Kurita K., Sugawara T., Nakamura K., Kasahara Y., Ogasawara N.,
RA Yamane K.;
RT "Determination of a 17,484 bp nucleotide sequence around the 39 degrees
RT region of the Bacillus subtilis chromosome and similarity analysis of the
RT products of putative ORFs.";
RL Microbiology 141:3241-3245(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA Medigue C., Rose M., Viari A., Danchin A.;
RT "Detecting and analyzing DNA sequencing errors: toward a higher quality of
RT the Bacillus subtilis genome sequence.";
RL Genome Res. 9:1116-1127(1999).
RN [5]
RP FUNCTION, PROBABLE INTERACTION WITH PXPC, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=9334321; DOI=10.1101/gad.11.19.2569;
RA Wang L., Grau R., Perego M., Hoch J.A.;
RT "A novel histidine kinase inhibitor regulating development in Bacillus
RT subtilis.";
RL Genes Dev. 11:2569-2579(1997).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND DISRUPTION PHENOTYPE.
RX PubMed=28830929; DOI=10.1074/jbc.m117.805028;
RA Niehaus T.D., Elbadawi-Sidhu M., de Crecy-Lagard V., Fiehn O., Hanson A.D.;
RT "Discovery of a widespread prokaryotic 5-oxoprolinase that was hiding in
RT plain sight.";
RL J. Biol. Chem. 292:16360-16367(2017).
RN [7] {ECO:0007744|PDB:2ZP2}
RP X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 100-240, AND INTERACTION WITH
RP KINA.
RX PubMed=18823995; DOI=10.1016/j.jmb.2008.09.017;
RA Jacques D.A., Langley D.B., Jeffries C.M., Cunningham K.A.,
RA Burkholder W.F., Guss J.M., Trewhella J.;
RT "Histidine kinase regulation by a cyclophilin-like inhibitor.";
RL J. Mol. Biol. 384:422-435(2008).
RN [8] {ECO:0007744|PDB:2KWA}
RP STRUCTURE BY NMR OF 1-99, AND INTERACTION WITH PXPC.
RX PubMed=21050859; DOI=10.1016/j.jmb.2010.10.047;
RA Jacques D.A., Langley D.B., Hynson R.M., Whitten A.E., Kwan A., Guss J.M.,
RA Trewhella J.;
RT "A novel structure of an antikinase and its inhibitor.";
RL J. Mol. Biol. 405:214-226(2011).
CC -!- FUNCTION: Catalyzes the cleavage of 5-oxoproline to form L-glutamate
CC coupled to the hydrolysis of ATP to ADP and inorganic phosphate
CC (PubMed:28830929). In addition, is a potent inhibitor of the
CC autophosphorylation reaction of kinase A (kinA) and its reverse
CC reaction, but does not inhibit phosphate transfer to the Spo0F response
CC regulator once kinase A is phosphorylated. Is an inhibitor of the
CC catalytic domain of kinase A affecting the ATP/ADP reactions and not
CC the phosphotransferase functions of this domain. The inhibition is non-
CC competitive with respect to ATP (PubMed:9334321).
CC {ECO:0000269|PubMed:28830929, ECO:0000269|PubMed:9334321}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=5-oxo-L-proline + ATP + 2 H2O = ADP + H(+) + L-glutamate +
CC phosphate; Xref=Rhea:RHEA:10348, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58402, ChEBI:CHEBI:456216; EC=3.5.2.9;
CC Evidence={ECO:0000269|PubMed:28830929};
CC -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC
CC (PubMed:28830929). Interacts with PxpC (KipA) (PubMed:9334321,
CC PubMed:21050859, PubMed:28830929). Interaction with PxpC prevents the
CC inhibitory action of PxpB (KipI) (PubMed:9334321, PubMed:21050859).
CC Interacts with KinA. Two PxpB monomers bind via their C-domains at a
CC conserved proline in the KinA dimerization and histidine-
CC phosphotransfer (DHp) domain (PubMed:18823995).
CC {ECO:0000269|PubMed:18823995, ECO:0000269|PubMed:21050859,
CC ECO:0000269|PubMed:28830929, ECO:0000269|PubMed:9334321}.
CC -!- INDUCTION: Induced by glucose when readily available sources of
CC nitrogen, such as ammonia or glutamine, are scarce. Transcriptionally
CC activated by TnrA and repressed by KipR. {ECO:0000269|PubMed:9334321}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene enhances sporulation
CC (PubMed:9334321). Deletion mutant grows less well than wild type on
CC minimal medium with ammonium as nitrogen source and cannot grow on 5-
CC oxoproline. Mutant lacks 5-oxoprolinase activity and accumulates 5-oxo-
CC L-proline (PubMed:28830929). {ECO:0000269|PubMed:28830929,
CC ECO:0000269|PubMed:9334321}.
CC -!- SIMILARITY: Belongs to the PxpB family. {ECO:0000305}.
CC -!- CAUTION: Was originally (PubMed:8574415 and PubMed:8969502) thought to
CC be a longer ORF that encodes what is now known to be pxpB (kipI) and
CC pxpC (kipA). {ECO:0000305|PubMed:9334321}.
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DR EMBL; D38161; BAA07361.1; ALT_SEQ; Genomic_DNA.
DR EMBL; D50453; BAA09039.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL009126; CAB12216.2; -; Genomic_DNA.
DR PIR; G69765; G69765.
DR RefSeq; NP_388290.2; NC_000964.3.
DR RefSeq; WP_003234420.1; NZ_JNCM01000031.1.
DR PDB; 2KWA; NMR; -; A=1-99.
DR PDB; 2ZP2; X-ray; 3.01 A; A/B=100-240.
DR PDBsum; 2KWA; -.
DR PDBsum; 2ZP2; -.
DR AlphaFoldDB; P60495; -.
DR BMRB; P60495; -.
DR SMR; P60495; -.
DR STRING; 224308.BSU04080; -.
DR PaxDb; P60495; -.
DR PRIDE; P60495; -.
DR EnsemblBacteria; CAB12216; CAB12216; BSU_04080.
DR GeneID; 938256; -.
DR KEGG; bsu:BSU04080; -.
DR PATRIC; fig|224308.179.peg.434; -.
DR eggNOG; COG2049; Bacteria.
DR InParanoid; P60495; -.
DR OMA; MPWMLAA; -.
DR PhylomeDB; P60495; -.
DR BioCyc; BSUB:BSU04080-MON; -.
DR BRENDA; 3.5.2.9; 658.
DR EvolutionaryTrace; P60495; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-EC.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004860; F:protein kinase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR Gene3D; 2.40.100.10; -; 1.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR010016; KipI_fam.
DR PANTHER; PTHR34698; PTHR34698; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SUPFAM; SSF50891; SSF50891; 1.
DR TIGRFAMs; TIGR00370; TIGR00370; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Hydrolase; Nucleotide-binding;
KW Protein kinase inhibitor; Reference proteome; Sporulation.
FT CHAIN 1..240
FT /note="5-oxoprolinase subunit B"
FT /id="PRO_0000084308"
FT BINDING 194..201
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT STRAND 6..9
FT /evidence="ECO:0007829|PDB:2KWA"
FT STRAND 11..18
FT /evidence="ECO:0007829|PDB:2KWA"
FT HELIX 25..40
FT /evidence="ECO:0007829|PDB:2KWA"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:2KWA"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:2KWA"
FT HELIX 62..66
FT /evidence="ECO:0007829|PDB:2KWA"
FT HELIX 76..88
FT /evidence="ECO:0007829|PDB:2KWA"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2KWA"
FT HELIX 93..95
FT /evidence="ECO:0007829|PDB:2KWA"
FT STRAND 101..109
FT /evidence="ECO:0007829|PDB:2ZP2"
FT TURN 110..112
FT /evidence="ECO:0007829|PDB:2ZP2"
FT HELIX 116..122
FT /evidence="ECO:0007829|PDB:2ZP2"
FT HELIX 127..134
FT /evidence="ECO:0007829|PDB:2ZP2"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:2ZP2"
FT STRAND 152..154
FT /evidence="ECO:0007829|PDB:2ZP2"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:2ZP2"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:2ZP2"
FT STRAND 183..186
FT /evidence="ECO:0007829|PDB:2ZP2"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:2ZP2"
FT STRAND 221..226
FT /evidence="ECO:0007829|PDB:2ZP2"
SQ SEQUENCE 240 AA; 26720 MW; CFD927E3A8E0FF5F CRC64;
MTVRYQIEQL GDSAMMIRFG EEINEQVNGI VHAAAAYIEE QPFPGFIECI PAFTSLTVFY
DMYEVYKHLP QGISSPFESV KRDVEERLAE IAEDYEVNRR IVEIPVCYGG EFGPDLEEVA
KINQLSPEEV IDIHTNGEYV VYMLGFAPGF PFLGGMSKRI AAPRKSSPRP SIPAGSVGIA
GLQTGVYPIS TPGGWQLIGK TPLALFRPQE NPPTLLRAGD IVKFVRISEK DYHAYKEESN
