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Database: UniProt
Entry: A0A378ASP5_KLEPO
LinkDB: A0A378ASP5_KLEPO
Original site: A0A378ASP5_KLEPO 
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
//
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