ID   PTRC_KLEPN              Reviewed;         266 AA.
AC   P37082;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   25-MAY-2022, entry version 80.
DE   RecName: Full=PTS system sorbose-specific EIIC component {ECO:0000303|PubMed:2287279};
DE   AltName: Full=EIIC-Sor {ECO:0000303|PubMed:2287279};
DE   AltName: Full=Sorbose permease IIC component {ECO:0000303|PubMed:2287279};
GN   Name=sorA {ECO:0000303|PubMed:2287279};
OS   Klebsiella pneumoniae.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX   NCBI_TaxID=573;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=1033-5P14 / KAY2026;
RX   PubMed=7947968; DOI=10.1016/0167-4838(94)90124-4;
RA   Wehmeier U.F., Lengeler J.W.;
RT   "Sequence of the sor-operon for L-sorbose utilization from Klebsiella
RT   pneumoniae KAY2026.";
RL   Biochim. Biophys. Acta 1208:348-351(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7700234; DOI=10.1007/bf00298968;
RA   Wehmeier U.F., Wohrl B.M., Lengeler J.W.;
RT   "Molecular analysis of the phosphoenolpyruvate-dependent L-sorbose:
RT   phosphotransferase system from Klebsiella pneumoniae and of its multidomain
RT   structure.";
RL   Mol. Gen. Genet. 246:610-618(1995).
RN   [3]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RC   STRAIN=1033-5P14 / KAY2026;
RX   PubMed=6361004; DOI=10.1128/jb.157.1.39-45.1984;
RA   Sprenger G.A., Lengeler J.W.;
RT   "L-Sorbose metabolism in Klebsiella pneumoniae and Sor+ derivatives of
RT   Escherichia coli K-12 and chemotaxis toward sorbose.";
RL   J. Bacteriol. 157:39-45(1984).
RN   [4]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=2287279; DOI=10.1111/j.1365-2958.1990.tb02067.x;
RA   Woehrl B.M., Lengeler J.W.;
RT   "Cloning and physical mapping of the sor genes for L-sorbose transport and
RT   metabolism from Klebsiella pneumoniae.";
RL   Mol. Microbiol. 4:1557-1565(1990).
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 SorABFM PTS
CC       system is involved in L-sorbose transport. {ECO:0000269|PubMed:6361004,
CC       ECO:0000305|PubMed:2287279, ECO:0000305|PubMed:7700234}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305|PubMed:6361004};
CC       Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU00429}.
CC   -!- INDUCTION: By L-sorbose. {ECO:0000269|PubMed:2287279}.
CC   -!- DOMAIN: The EIIC type-4 domain forms the PTS system translocation
CC       channel and contains the specific substrate-binding site.
CC       {ECO:0000255|PROSITE-ProRule:PRU00429}.
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DR   EMBL; X66059; CAA46859.1; -; Genomic_DNA.
DR   PIR; S50189; S50189.
DR   AlphaFoldDB; P37082; -.
DR   SMR; P37082; -.
DR   TCDB; 4.A.6.1.3; the pts mannose-fructose-sorbose (man) family.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   InterPro; IPR004700; PTS_IIC_man.
DR   Pfam; PF03609; EII-Sor; 1.
DR   TIGRFAMs; TIGR00822; EII-Sor; 1.
DR   PROSITE; PS51106; PTS_EIIC_TYPE_4; 1.
PE   2: Evidence at transcript level;
KW   Cell inner membrane; Cell membrane; Membrane; Phosphotransferase system;
KW   Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..266
FT                   /note="PTS system sorbose-specific EIIC component"
FT                   /id="PRO_0000186663"
FT   TRANSMEM        3..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TRANSMEM        33..53
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TRANSMEM        79..99
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TRANSMEM        100..120
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TRANSMEM        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TRANSMEM        183..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
FT   DOMAIN          1..237
FT                   /note="PTS EIIC type-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00429"
SQ   SEQUENCE   266 AA;  27872 MW;  504FD32A4F268FBC CRC64;
     MEISTLQIIA IFIFSCIAGM GSVLDEFQTH RPLIACTVIG LILGDLKTGV MLGGTLELIA
     LGWMNVGAAQ SPDSALASII SAILVIVGHQ SIAIGIAIAL PVAAAGQVLT VFARTITVVF
     QHAADKAAEE ARFRTIDLLH VSALGVQGLR VAIPALVVSL FVSADMVSSM LSAIPEFVTR
     GLQIAGGFIV VVGYAMVLRM MGVKYLMPFF FLGFLAGGYL DFSLLAFGGV GVIIALIYIQ
     LNPQWRKAEP AASTAPSAPA LDQLDD