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Database: UniProt
Entry: A7MIQ5_CROS8
LinkDB: A7MIQ5_CROS8
Original site: A7MIQ5_CROS8 
ID   A7MIQ5_CROS8            Unreviewed;       492 AA.
AC   A7MIQ5;
DT   02-OCT-2007, integrated into UniProtKB/TrEMBL.
DT   02-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABU78742.1};
GN   OrderedLocusNames=ESA_03527 {ECO:0000313|EMBL:ABU78742.1};
OS   Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Cronobacter.
OX   NCBI_TaxID=290339 {ECO:0000313|EMBL:ABU78742.1, ECO:0000313|Proteomes:UP000000260};
RN   [1] {ECO:0000313|EMBL:ABU78742.1, ECO:0000313|Proteomes:UP000000260}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-894 {ECO:0000313|EMBL:ABU78742.1,
RC   ECO:0000313|Proteomes:UP000000260};
RX   PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA   Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA   Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA   Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA   McClelland M., Forsythe S.J.;
RT   "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT   hybridization analysis with other Cronobacter species.";
RL   PLoS ONE 5:E9556-E9556(2010).
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000783; ABU78742.1; -; Genomic_DNA.
DR   AlphaFoldDB; A7MIQ5; -.
DR   KEGG; esa:ESA_03527; -.
DR   HOGENOM; CLU_012312_2_0_6; -.
DR   Proteomes; UP000000260; Chromosome.
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:UniProtKB-KW.
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   InterPro; IPR010973; PTS_IIBC_sucr.
DR   InterPro; IPR004719; PTS_maltose/Glc_sub_IIC.
DR   NCBIfam; TIGR00826; EIIB_glc; 1.
DR   NCBIfam; TIGR00852; pts-Glc; 1.
DR   NCBIfam; TIGR01996; PTS-II-BC-sucr; 1.
DR   PANTHER; PTHR30175:SF7; NEGATIVE REGULATOR OF SACY ACTIVITY; 1.
DR   PANTHER; PTHR30175; PHOSPHOTRANSFERASE SYSTEM TRANSPORT PROTEIN; 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:UP000000260};
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..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        181..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        214..237
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        249..269
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..344
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        365..386
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        398..416
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        428..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        464..485
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          40..123
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51098"
FT   DOMAIN          143..492
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000259|PROSITE:PS51103"
FT   ACT_SITE        62
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   492 AA;  51890 MW;  6CC1CA32D7B195D1 CRC64;
     MELRRTDGNL VLIKRPLPRG GLRIVDNIKN HKTEVVMDFE QIARSLLPLL GGKENIASAA
     HCATRLRLVL VDDAKADTAA IGNVEGVKGC FRNAGQLQII FGTGVVNKVY AAFITVAGIS
     ESSKSEAASV AARKLNPFQR IARLLSNIFV PIIPAIVASG LLMGLLGMVK TYGWVSPDNA
     LYIMLDMCSS AAFIILPILI GFTAAREFGG NPYLGATLGG ILTHPALTNA WGVAAGFHTM
     NFFGIEVAMI GYQGTVFPVL LAVWFMSILE KQLRRIIPDA LDLILTPFFT VIISGFVALL
     VIGPAGRALG DGISLVLSTL ITHAGWLAGL LFGGLYSVIV ITGVHHSFHA IEAGLLGNPS
     IGVNFLLPIW AMANVAQGGA CLAVWFKTKD AKVKAITLPS GFSALLGITE AAIFGVNLRF
     VKPFISGLIG GAAGGAWVVS THVGMTAVGL TGIPGMAIVQ ASSLLNYVIG MAIAFCIAFA
     VSYLWKYKTD AE
//
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