ID   CNTK_STAAM              Reviewed;         273 AA.
AC   A0A0H3JU78;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   16-SEP-2015, sequence version 1.
DT   03-AUG-2022, entry version 21.
DE   RecName: Full=Histidine racemase {ECO:0000303|PubMed:27230378};
DE            EC=5.1.1.24 {ECO:0000269|PubMed:27230378};
GN   Name=cntK {ECO:0000303|PubMed:27230378};
GN   OrderedLocusNames=SAV2470 {ECO:0000312|EMBL:BAB58632.1};
OS   Staphylococcus aureus (strain Mu50 / ATCC 700699).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158878;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND INDUCTION.
RC   STRAIN=Mu50 / ATCC 700699;
RX   PubMed=27230378; DOI=10.1126/science.aaf1018;
RA   Ghssein G., Brutesco C., Ouerdane L., Fojcik C., Izaute A., Wang S.,
RA   Hajjar C., Lobinski R., Lemaire D., Richaud P., Voulhoux R., Espaillat A.,
RA   Cava F., Pignol D., Borezee-Durant E., Arnoux P.;
RT   "Biosynthesis of a broad-spectrum nicotianamine-like metallophore in
RT   Staphylococcus aureus.";
RL   Science 352:1105-1109(2016).
CC   -!- FUNCTION: Catalyzes the reversible interconversion of the L- and D-
CC       stereoisomers of histidine. Functions in the biosynthesis of the
CC       metallophore staphylopine, which is involved in the acquisition of
CC       nickel, cobalt, zinc, copper, and iron, and thus enables bacterial
CC       growth inside the host, where metal access is limited. Therefore, this
CC       enzyme probably contributes to staphylococcal virulence. Appears to be
CC       specific for histidine, as it cannot use L-alanine and L-methionine as
CC       substrate. {ECO:0000269|PubMed:27230378}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-histidine = D-histidine; Xref=Rhea:RHEA:59188,
CC         ChEBI:CHEBI:57595, ChEBI:CHEBI:142967; EC=5.1.1.24;
CC         Evidence={ECO:0000269|PubMed:27230378};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:59189;
CC         Evidence={ECO:0000305|PubMed:27230378};
CC   -!- INDUCTION: Up-regulated in metal-poor media.
CC       {ECO:0000269|PubMed:27230378}.
CC   -!- SIMILARITY: Belongs to the histidine racemase family. {ECO:0000305}.
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DR   EMBL; BA000017; BAB58632.1; -; Genomic_DNA.
DR   RefSeq; WP_001081693.1; NC_002758.2.
DR   AlphaFoldDB; A0A0H3JU78; -.
DR   SMR; A0A0H3JU78; -.
DR   PaxDb; A0A0H3JU78; -.
DR   EnsemblBacteria; BAB58632; BAB58632; SAV2470.
DR   KEGG; sav:SAV2470; -.
DR   HOGENOM; CLU_087271_0_0_9; -.
DR   OMA; GNACMAL; -.
DR   BioCyc; SAUR158878:SAV_RS13480-MON; -.
DR   Proteomes; UP000002481; Chromosome.
DR   GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Isomerase.
FT   CHAIN           1..273
FT                   /note="Histidine racemase"
FT                   /id="PRO_0000447033"
SQ   SEQUENCE   273 AA;  31004 MW;  515F6E6CE57C6B1F CRC64;
     MNRQVIEFSK YNPSGNMTIL VHSKHDASEY ASIANQLMAA THVCCEQVGF IESTQNDDGN
     DFHLVMSGNE FCGNATMSYI HHLQESHLLK DQQFKVKVSG CSDLVQCAIH DCQYYEVQMP
     QAHRVVPTTI NMGNHSWKAL EIIYETYVHY VIPVKQVTTE IQHLVEAFVR EQQWSHKYKT
     VGMMLFDEQR QFLQPLIYIP EIQSLIWENS CGSGTASIGV FNNYQRNDAC KDFTVHQPGG
     SILVTSKRCH QLGYQTSIKG QVTTVATGKA YIE