ID   PTRA_LACCA              Reviewed;         138 AA.
AC   Q9RGG5; F2M4U9;
DT   05-OCT-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=PTS system sorbose-specific EIIA component {ECO:0000303|PubMed:10613875};
DE   AltName: Full=EIIA-Sor {ECO:0000303|PubMed:10613875};
DE   AltName: Full=Sorbose-specific phosphotransferase enzyme IIA component {ECO:0000303|PubMed:10613875};
GN   Name=sorA {ECO:0000303|PubMed:10613875};
OS   Lactobacillus casei.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=1582;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP   SUBCELLULAR LOCATION, INDUCTION, AND PHOSPHORYLATION AT HIS-8.
RC   STRAIN=ATCC 393 / DSM 20011 / BCRC 10697 / JCM 1134 / NBRC 15883 / NCIMB
RC   11970 / NCDO 161 / WDCM 00100;
RX   PubMed=10613875; DOI=10.1128/jb.182.1.155-163.2000;
RA   Yebra M.J., Veyrat A., Santos M.A., Perez-Martinez G.;
RT   "Genetics of L-sorbose transport and metabolism in Lactobacillus casei.";
RL   J. Bacteriol. 182:155-163(2000).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), a major carbohydrate active transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane. The enzyme II SorABCD PTS
CC       system is involved in L-sorbose transport.
CC       {ECO:0000269|PubMed:10613875}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:10613875}.
CC   -!- INDUCTION: Induced by L-sorbose and repressed by D-glucose.
CC       {ECO:0000269|PubMed:10613875}.
CC   -!- DOMAIN: The EIIA type-4 domain is phosphorylated by phospho-HPr on a
CC       histidyl residue. Then, it transfers the phosphoryl group to the EIIB
CC       type-4 domain. {ECO:0000255|PROSITE-ProRule:PRU00419}.
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DR   EMBL; AF129168; AAF24131.1; -; Genomic_DNA.
DR   RefSeq; WP_012490965.1; NZ_MODT01000074.1.
DR   AlphaFoldDB; Q9RGG5; -.
DR   SMR; Q9RGG5; -.
DR   STRING; 543734.LCABL_04250; -.
DR   TCDB; 4.A.6.1.26; the pts mannose-fructose-sorbose (man) family.
DR   iPTMnet; Q9RGG5; -.
DR   eggNOG; COG2893; Bacteria.
DR   OMA; VNANSMD; -.
DR   BRENDA; 2.7.1.206; 2854.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00006; PTS_IIA_man; 1.
DR   Gene3D; 3.40.50.510; -; 1.
DR   InterPro; IPR013789; PTS_EIIA_man.
DR   InterPro; IPR004701; PTS_EIIA_man-typ.
DR   InterPro; IPR036662; PTS_EIIA_man-typ_sf.
DR   InterPro; IPR033887; PTS_IIA_man.
DR   Pfam; PF03610; EIIA-man; 1.
DR   SUPFAM; SSF53062; SSF53062; 1.
DR   TIGRFAMs; TIGR00824; EIIA-man; 1.
DR   PROSITE; PS51096; PTS_EIIA_TYPE_4; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..138
FT                   /note="PTS system sorbose-specific EIIA component"
FT                   /id="PRO_0000437530"
FT   DOMAIN          1..125
FT                   /note="PTS EIIA type-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00419"
FT   ACT_SITE        8
FT                   /note="Tele-phosphohistidine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00419,
FT                   ECO:0000305|PubMed:10613875"
FT   MOD_RES         8
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000305|PubMed:10613875"
SQ   SEQUENCE   138 AA;  14985 MW;  16CFDE0FEEAD75DC CRC64;
     MEIILVGHAH TAKAFKEAVE MIYGEVPNFH PIDFTPKEGL QSLTDKIVSA IEPGKTASTL
     IITDLFSGTP YNASAELVLK KKAADVVAGM CLPMLLEVAV NANNMSVSQL VSHLMKIKEE
     FSTSLSEKMT TNAKEDDF