ID   4HYPE_BRUSI             Reviewed;         333 AA.
AC   A9WWR5;
DT   25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=4-hydroxyproline epimerase;
DE            EC=5.1.1.8;
DE   AltName: Full=Hydroxyproline-2-epimerase;
DE            Short=HyPRE;
GN   OrderedLocusNames=BSUIS_B1268;
OS   Brucella suis (strain ATCC 23445 / NCTC 10510).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=470137;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23445 / NCTC 10510;
RA   Setubal J.C., Bowns C., Boyle S., Crasta O.R., Czar M.J., Dharmanolla C.,
RA   Gillespie J.J., Kenyon R.W., Lu J., Mane S., Mohapatra S., Nagrani S.,
RA   Purkayastha A., Rajasimha H.K., Shallom J.M., Shallom S., Shukla M.,
RA   Snyder E.E., Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H.,
RA   Bruce D., Detter C., Munk C., Brettin T.S.;
RT   "Brucella suis ATCC 23445 whole genome shotgun sequencing project.";
RL   Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
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). {ECO:0000250}.
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; CP000912; ABY40201.1; -; Genomic_DNA.
DR   RefSeq; WP_006074544.1; NC_010167.1.
DR   AlphaFoldDB; A9WWR5; -.
DR   SMR; A9WWR5; -.
DR   EnsemblBacteria; ABY40201; ABY40201; BSUIS_B1268.
DR   KEGG; bmt:BSUIS_B1268; -.
DR   HOGENOM; CLU_036729_0_0_5; -.
DR   OMA; SHVLWTG; -.
DR   Proteomes; UP000008545; Chromosome II.
DR   GO; GO:0047580; F:4-hydroxyproline epimerase activity; IEA:UniProtKB-EC.
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   3: Inferred from homology;
KW   Isomerase.
FT   CHAIN           1..333
FT                   /note="4-hydroxyproline epimerase"
FT                   /id="PRO_0000354031"
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"
SQ   SEQUENCE   333 AA;  36593 MW;  0963CC7E039F5717 CRC64;
     MARHSFFCVD GHTCGNPVRL VAGGGPNLNG STMMEKRAHF LAEYDWIRTG LMFEPRGHDM
     MSGSILYPPT RPDCDVAVLF IETSGCLPMC GHGTIGTVTM AIEQGLVTPK TPGKLNLDTP
     AGLVAIEYEQ DGQYVERVRL TNVPAFLYAE GLEVECPDLG PIKVDVAYGG NFYAIVEPQE
     NYTDMDDYSA LQLIAWSPVL RQRLNEKYKF QHPELPDINR LSHILWTGKP EHPQAHARNA
     VFYGDKAIDR SPCGTGTSAR MAQLAAKGKL KPGDEFIHES IIGSLFHGRV ERAAEVAGRP
     AIVPSIAGWA RMTGYNTIFI DDRDPFAHGF SVA