ID A0KIG4_AERHH Unreviewed; 484 AA.
AC A0KIG4;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=Pts system, N-acetylglucosamine-specific iibc component {ECO:0000313|EMBL:ABK38509.1};
DE EC=2.7.1.69 {ECO:0000313|EMBL:ABK38509.1};
GN Name=nagE {ECO:0000313|EMBL:ABK38509.1};
GN OrderedLocusNames=AHA_1527 {ECO:0000313|EMBL:ABK38509.1};
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK38509.1, ECO:0000313|Proteomes:UP000000756};
RN [1] {ECO:0000313|EMBL:ABK38509.1, ECO:0000313|Proteomes:UP000000756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC KCTC 2358 / NCIMB 9240 / NCTC 8049
RC {ECO:0000313|Proteomes:UP000000756};
RX PubMed=16980456; DOI=10.1128/JB.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP000462; ABK38509.1; -; Genomic_DNA.
DR RefSeq; WP_011705424.1; NC_008570.1.
DR RefSeq; YP_856065.1; NC_008570.1.
DR AlphaFoldDB; A0KIG4; -.
DR STRING; 380703.AHA_1527; -.
DR EnsemblBacteria; ABK38509; ABK38509; AHA_1527.
DR GeneID; 77274881; -.
DR KEGG; aha:AHA_1527; -.
DR PATRIC; fig|380703.7.peg.1540; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_6; -.
DR OrthoDB; 7571469at2; -.
DR Proteomes; UP000000756; Chromosome.
DR GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0103111; F:D-glucosamine PTS permease activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015572; F:N-acetylglucosamine transmembrane transporter activity; IEA:InterPro.
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; IPR010974; PTS_IIBC_nag.
DR NCBIfam; TIGR00826; EIIB_glc; 1.
DR NCBIfam; TIGR01998; PTS-II-BC-nag; 1.
DR PANTHER; PTHR30009; CYTOCHROME C-TYPE SYNTHESIS PROTEIN AND PTS TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR30009:SF4; PTS SYSTEM N-ACETYLGLUCOSAMINE-SPECIFIC EIICBA 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:UP000000756};
KW Sugar transport {ECO:0000256|ARBA:ARBA00022597};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ABK38509.1};
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 12..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 82..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 115..135
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 155..178
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 284..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..382
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..394
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 408..484
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT ACT_SITE 430
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 484 AA; 51418 MW; 4CE1D0262E7CBDC6 CRC64;
MNILGYLQKI GRALMVPVAV LPAAAILMGI GYWIDPNGWG GGSPVAAFLI KAGAAIIDSM
PVLFAVGVAY GMSKDKDGSA ALAGLVGFLV VTTLLSPGAV AQIKGIPADQ VPAAFAKISN
QFVGILCGVI AAELYNRFSS VELHKALAFF SGRRLVPIVT SVVMIVVSFI LMAVWPVIYG
GLVSFGESIV SLGSTGAGIY AFFNRLLIPV GLHHALNSVF WFDVAGINDI PNFLGGQSSI
DAGKGIVGVT GMYQAGFFPI MMFGLPGAAL AIYHSAKKEN KEKVASIMIA AAFAAFFTGV
TEPLEFSFMF VAPVLYVIHA LLTGLSVFIA ASMQWIAGFG FSAGLVDMVL SSRNPLATHW
YMLLVQGLVF FGLYYVVFRA VIVKFNLKTP GREDDEAVPA QAQTTDRTEL ARQYLEVLGG
QENLVTIDAC ITRLRLTLKD RSIVDERKLK ALGAAGVVKL GEQNLQVILG PLAEIIAGEM
KALR
//
