PXPA_BACSU
ID PXPA_BACSU Reviewed; 257 AA.
AC P42963;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 4.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=5-oxoprolinase subunit A {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000305};
DE Short=5-OPase subunit A {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000305};
DE EC=3.5.2.9 {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000269|PubMed:28830929};
DE AltName: Full=5-oxoprolinase (ATP-hydrolyzing) subunit A {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000305};
GN Name=pxpA {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000303|PubMed:28830929};
GN Synonyms=ycsF; OrderedLocusNames=BSU04050;
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=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 [2]
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 [3]
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 [4]
RP SEQUENCE REVISION TO 208 AND 219-224.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 46-257.
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 [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).
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 {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000269|PubMed:28830929}.
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:0000255|HAMAP-Rule:MF_00691,
CC ECO:0000269|PubMed:28830929};
CC -!- SUBUNIT: Forms a complex composed of PxpA, PxpB and PxpC.
CC {ECO:0000255|HAMAP-Rule:MF_00691, ECO:0000269|PubMed:28830929}.
CC -!- DISRUPTION PHENOTYPE: 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. {ECO:0000269|PubMed:28830929}.
CC -!- SIMILARITY: Belongs to the LamB/PxpA family. {ECO:0000255|HAMAP-
CC Rule:MF_00691, ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA07357.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA09036.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D50453; BAA09036.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AL009126; CAB12213.3; -; Genomic_DNA.
DR EMBL; D38161; BAA07357.1; ALT_FRAME; Genomic_DNA.
DR PIR; D69765; D69765.
DR RefSeq; NP_388287.3; NC_000964.3.
DR RefSeq; WP_003234423.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; P42963; -.
DR SMR; P42963; -.
DR STRING; 224308.BSU04050; -.
DR PaxDb; P42963; -.
DR PRIDE; P42963; -.
DR EnsemblBacteria; CAB12213; CAB12213; BSU_04050.
DR GeneID; 938259; -.
DR KEGG; bsu:BSU04050; -.
DR PATRIC; fig|224308.179.peg.431; -.
DR eggNOG; COG1540; Bacteria.
DR InParanoid; P42963; -.
DR OMA; DRTYKQD; -.
DR PhylomeDB; P42963; -.
DR BioCyc; BSUB:BSU04050-MON; -.
DR BRENDA; 3.5.2.9; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0017168; F:5-oxoprolinase (ATP-hydrolyzing) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IBA:GO_Central.
DR HAMAP; MF_00691; PxpA; 1.
DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl.
DR InterPro; IPR005501; LamB/YcsF/PxpA-like.
DR PANTHER; PTHR30292; PTHR30292; 1.
DR Pfam; PF03746; LamB_YcsF; 1.
DR SUPFAM; SSF88713; SSF88713; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT CHAIN 1..257
FT /note="5-oxoprolinase subunit A"
FT /id="PRO_0000184990"
FT CONFLICT 208
FT /note="S -> F (in Ref. 1; BAA09036 and 5; BAA07357)"
FT /evidence="ECO:0000305"
FT CONFLICT 219..224
FT /note="DTVCIH -> GSVFIY (in Ref. 1; BAA09036 and 5;
FT BAA07357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 257 AA; 27482 MW; 2799684330644E71 CRC64;
MFQIDLNCDL GESFGAYKIG LDQDILEYVT SANIACGFHA GDPSVMRKTV ALAAERGVKM
GAHPGLPDLL GFGRRNMAIS PEEAYDLVVY QIGALSGFLK AEGLHMQHVK PHGALYNMAA
VDQKLSDAIA KAVYKVDPGL ILFGLAESEL VKAGERIGLQ TANEVFADRT YQSDGTLTPR
SQPDALIESD DAAVTQVIKM VKEGAVKSQQ GHDVSLKADT VCIHGDGAHA LTFAQKIRKQ
LKAAGIEVTA ISEQRST
