ID A0A378ASP5_KLEPO Unreviewed; 549 AA.
AC A0A378ASP5;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE RecName: Full=PTS system lactose-specific EIICB component {ECO:0000256|ARBA:ARBA00020834};
DE EC=2.7.1.207 {ECO:0000256|ARBA:ARBA00012802};
DE AltName: Full=EIICB-Lac {ECO:0000256|ARBA:ARBA00029639};
GN Name=gmuC_4 {ECO:0000313|EMBL:STV20226.1};
GN ORFNames=NCTC5050_03104 {ECO:0000313|EMBL:STV20226.1};
OS Klebsiella pneumoniae subsp. ozaenae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=574 {ECO:0000313|EMBL:STV20226.1, ECO:0000313|Proteomes:UP000255382};
RN [1] {ECO:0000313|EMBL:STV20226.1, ECO:0000313|Proteomes:UP000255382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC5050 {ECO:0000313|EMBL:STV20226.1,
RC ECO:0000313|Proteomes:UP000255382};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lactose(out) + N(pros)-phospho-L-histidyl-[protein] = L-
CC histidyl-[protein] + lactose 6-phosphate(in); Xref=Rhea:RHEA:42400,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:17716,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:64837, ChEBI:CHEBI:79080;
CC EC=2.7.1.207; Evidence={ECO:0000256|ARBA:ARBA00001568};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; UGLZ01000005; STV20226.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A378ASP5; -.
DR Proteomes; UP000255382; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05564; PTS_IIB_chitobiose_lichenan; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR013012; PTS_EIIB_3.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR004501; PTS_EIIC_3.
DR NCBIfam; TIGR00410; lacE; 1.
DR PANTHER; PTHR33989; -; 1.
DR PANTHER; PTHR33989:SF4; PTS SYSTEM N,N'-DIACETYLCHITOBIOSE-SPECIFIC EIIC COMPONENT; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR PROSITE; PS51100; PTS_EIIB_TYPE_3; 1.
DR PROSITE; PS51105; PTS_EIIC_TYPE_3; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000255382};
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 144..163
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 189..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 221..239
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 251..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 339..361
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 397..415
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 496..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..102
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000259|PROSITE:PS51100"
FT DOMAIN 121..522
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000259|PROSITE:PS51105"
FT MOD_RES 8
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00423"
SQ SEQUENCE 549 AA; 60273 MW; 43EE742F190840E7 CRC64;
MYKIMLCCSA GMSTSLLVRK MVEAANERDL SVQIDAYGVS EFDMQFPQYQ VVLLGPQVKY
MLKTLSDKAA SLNIPVQPID TMDYGMQRGR QRPELCSVAD PSGALRGVEM SSLYQSMIAV
IEQSITPLAG RLGQQKYVIA IRDGFTAALP FMIIGSFMLV FIFPPFSPDT TNGFARGWLD
FSQHYREQLM LPFNLSMGVM TFFISVGIGA SLGRQFQLDP VMSGLLAFMA FLLVAAPYAD
GKISTQYLSG QGIFTALITA IYSTRVYAWL KQNNITIRLP KEVPTGVARS FEILIPVLVV
IATLHPLNLF IEAQTGMILP QAIMHLLEPL VSASDSLPAI LLSVLMCQIF WFAGIHGSLI
VTGIMNPFWM ANLSANQAAL AAGTVLPHVY LQGFWDHYLL IGGVGSTLPL AFLLLRSRAT
HLRTIGKMGI VPSFFNINEP ILFGAPIIMN PMMFIPFVCV PMVNAVLAYG ATRLGWLSQV
VSLTPWTTPA PIGASWAANW TLSPVVMCLI CMVMSAVIYL PFLRAYERSL MKTEVEKAKN
SVPVAETVS
//