ID   4HYPE_BRUA2             Reviewed;         333 AA.
AC   Q2YLF3;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 73.
DE   RecName: Full=4-hydroxyproline epimerase;
DE            EC=5.1.1.8;
DE   AltName: Full=Hydroxyproline-2-epimerase;
DE            Short=HyPRE;
GN   Name=prpA; OrderedLocusNames=BAB1_1800;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
RN   [2]
RP   ROLE IN VIRULENCE, AND MUTAGENESIS OF CYS-253.
RX   PubMed=17053080; DOI=10.1073/pnas.0603362103;
RA   Spera J.M., Ugalde J.E., Mucci J., Comerci D.J., Ugalde R.A.;
RT   "A B lymphocyte mitogen is a Brucella abortus virulence factor required for
RT   persistent infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:16514-16519(2006).
CC   -!- FUNCTION: Allows intracellular utilization of 4-hydroxyproline, one of
CC       the major constituents of host collagen, by converting 4-hydroxy-L-
CC       proline to 4-hydroxy-D-proline, which can be further metabolized by
CC       intracellular 4-hydroxy-D-proline oxidases. Strong B-cell mitogen.
CC       Plays an important role in the regulation of intra- and extracellular
CC       amino acid pools, allowing the bacterium to profit from host precursors
CC       and enzymatic pathways (By similarity). Directly involved in the immune
CC       regulation of host. Elicits B-lymphocyte polyclonal activation,
CC       resulting in early and transient nonresponsive immune condition of the
CC       host. {ECO:0000250, ECO:0000269|PubMed:17053080}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=trans-4-hydroxy-L-proline = cis-4-hydroxy-D-proline;
CC         Xref=Rhea:RHEA:21152, ChEBI:CHEBI:57690, ChEBI:CHEBI:58375;
CC         EC=5.1.1.8;
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the proline racemase family. {ECO:0000305}.
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DR   EMBL; AM040264; CAJ11756.1; -; Genomic_DNA.
DR   RefSeq; WP_002964871.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YLF3; -.
DR   SMR; Q2YLF3; -.
DR   STRING; 359391.BAB1_1800; -.
DR   EnsemblBacteria; CAJ11756; CAJ11756; BAB1_1800.
DR   GeneID; 3788305; -.
DR   KEGG; bmf:BAB1_1800; -.
DR   PATRIC; fig|359391.11.peg.312; -.
DR   HOGENOM; CLU_036729_0_0_5; -.
DR   OMA; SHVLWTG; -.
DR   PhylomeDB; Q2YLF3; -.
DR   BRENDA; 5.1.1.8; 994.
DR   Proteomes; UP000002719; Chromosome I.
DR   GO; GO:0047580; F:4-hydroxyproline epimerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042116; P:macrophage activation; IDA:CACAO.
DR   InterPro; IPR008794; Pro_racemase_fam.
DR   PANTHER; PTHR33442; PTHR33442; 1.
DR   Pfam; PF05544; Pro_racemase; 1.
DR   PIRSF; PIRSF029792; Pro_racemase; 1.
DR   SFLD; SFLDS00028; Proline_Racemase; 1.
PE   1: Evidence at protein level;
KW   Isomerase; Reference proteome.
FT   CHAIN           1..333
FT                   /note="4-hydroxyproline epimerase"
FT                   /id="PRO_0000354026"
FT   ACT_SITE        90
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   ACT_SITE        253
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         91..92
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         249
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   BINDING         254..255
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q4KGU2"
FT   MUTAGEN         253
FT                   /note="C->T: Loss of function; loss of mitogenic activity
FT                   on mouse splenocytes."
FT                   /evidence="ECO:0000269|PubMed:17053080"
SQ   SEQUENCE   333 AA;  36670 MW;  34DA2AA5674D5FB9 CRC64;
     MARHSFFCVD GHTCGNPVRL VAGGGPNLNG STMMEKRAHF LAEYDWIRTG LMFEPRGHDM
     MSGSILYPPT RPDCDVAVLF IETSGCLPMC GHGTIGTVTM AIEQGLVTPK TPGKLNLDTP
     AGLVAIEYEQ DGQYVERVRL TNVPAFLYAE GLEVECPDLG PIKVDVAYGG NFYAIVEPQE
     NYTDMDDYSA LQLIAWSPVL RQRLNEKYKF QHPELPDINR LSHILWTGKP KHPQAHARNA
     VFYGDKAIDR SPCGTGTSAR MAQLAAKGKL KPCDEFIHES IIGSLFHGRV ERAAEVAGRP
     AIVPSIAGWA RMTGYNTIFI DDRDPFAHGF SMA