ID Q8ZN26_SALTY Unreviewed; 453 AA.
AC Q8ZN26;
DT 01-MAR-2002, integrated into UniProtKB/TrEMBL.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 138.
DE RecName: Full=PTS system N-acetylmuramic acid-specific EIIBC component {ECO:0000256|ARBA:ARBA00040399};
DE EC=2.7.1.192 {ECO:0000256|ARBA:ARBA00039021};
DE AltName: Full=EIIBC-MurNAc {ECO:0000256|ARBA:ARBA00043021};
GN OrderedLocusNames=STM2570 {ECO:0000313|EMBL:AAL21464.1};
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287 {ECO:0000313|EMBL:AAL21464.1, ECO:0000313|Proteomes:UP000001014};
RN [1] {ECO:0000313|EMBL:AAL21464.1, ECO:0000313|Proteomes:UP000001014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720
RC {ECO:0000313|Proteomes:UP000001014};
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(pros)-phospho-L-histidyl-[protein] + N-acetyl-beta-D-
CC muramate(out) = L-histidyl-[protein] + N-acetyl-beta-D-muramate 6-
CC phosphate(in); Xref=Rhea:RHEA:33399, Rhea:RHEA-COMP:9745, Rhea:RHEA-
CC COMP:9746, ChEBI:CHEBI:29979, ChEBI:CHEBI:58721, ChEBI:CHEBI:64837,
CC ChEBI:CHEBI:64848; EC=2.7.1.192;
CC Evidence={ECO:0000256|ARBA:ARBA00036529};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; AE006468; AAL21464.1; -; Genomic_DNA.
DR RefSeq; NP_461505.1; NC_003197.2.
DR RefSeq; WP_000361663.1; NC_003197.2.
DR AlphaFoldDB; Q8ZN26; -.
DR STRING; 99287.STM2570; -.
DR PaxDb; 99287-STM2570; -.
DR GeneID; 1254092; -.
DR KEGG; stm:STM2570; -.
DR PATRIC; fig|99287.12.peg.2711; -.
DR HOGENOM; CLU_012312_2_0_6; -.
DR OMA; RFHKWLP; -.
DR PhylomeDB; Q8ZN26; -.
DR BioCyc; SENT99287:STM2570-MONOMER; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0090588; F:protein-phosphocysteine-N-acetylmuramate phosphotransferase system transporter activity; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 3.30.1360.60; Glucose permease domain IIB; 1.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 1.
DR PANTHER; PTHR30175:SF3; PTS SYSTEM N-ACETYLMURAMIC ACID-SPECIFIC EIIBC COMPONENT; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; Glucose permease domain IIB; 1.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphotransferase system {ECO:0000256|ARBA:ARBA00022683};
KW Reference proteome {ECO:0000313|Proteomes:UP000001014};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 115..136
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..176
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 188..208
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 214..231
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 325..345
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 357..378
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..447
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..88
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 113..453
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT ACT_SITE 27
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 453 AA; 47247 MW; C7A8DEB114B29DD2 CRC64;
MDKTAALASD ILRGIGGEQN ILRLENCMTR VRVEVQDDSQ LDIPRLKALP GVSGYVKQGE
QHQLIVGPGK AAQVVDAMRV QIAAGGVKPD DAMARTKSEA KAKYKAPMSD ALRKLANVFI
PLIPAFIASG LITGIINILK RPDIVGDVAV HYPNLLGLMG IFGSAVFAIM NILVGVNTAK
VFGGSQALGG VMAGILSSPQ LAQITLFGEV LQPGRGGVIA VLLVVALMCW IERQFRKLLP
GSLELILNPL LTTVITGAVA IVALQPLGGW ISDAIAHGAS WAIDRGGFLV GAVLAGTFLP
LVLTGLHQGL VPIHVELVQA HGYNALFPIL AMAGVGQIGA AIAVLMKTRN ARLKKVIKGA
LPVGLLGIGE PLIFGVTLPL GKPFIGACLG GAVGGALISY WKVATVITFG ISGLPLALTI
VAGKVLFYLL GYLIAVIAGF IFTWLLGFND PEE
//
