ID D0LVP8_HALO1 Unreviewed; 603 AA.
AC D0LVP8;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE SubName: Full=PTS system, glucose-like IIB subunint {ECO:0000313|EMBL:ACY14032.1};
GN OrderedLocusNames=Hoch_1479 {ECO:0000313|EMBL:ACY14032.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY14032.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY14032.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00421}.
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DR EMBL; CP001804; ACY14032.1; -; Genomic_DNA.
DR RefSeq; WP_012826641.1; NC_013440.1.
DR AlphaFoldDB; D0LVP8; -.
DR STRING; 502025.Hoch_1479; -.
DR KEGG; hoh:Hoch_1479; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_1_0_7; -.
DR Proteomes; UP000001880; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; 2.
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 NCBIfam; TIGR00826; EIIB_glc; 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; 2.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; Glucose permease domain IIB; 2.
DR PROSITE; PS51098; PTS_EIIB_TYPE_1; 2.
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:UP000001880};
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 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 46..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 71..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 110..131
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 143..164
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..195
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 207..225
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 271..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 348..367
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..379
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000259|PROSITE:PS51103"
FT DOMAIN 408..490
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT DOMAIN 522..603
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000259|PROSITE:PS51098"
FT REGION 494..515
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 430
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 603 AA; 63062 MW; 4871C458BF678223 CRC64;
MLEFLQRIGR SLMLPIAVMP AAALLMRLGA PDVLDLPFIQ AAGSEIFVYL PLLFAAGIVI
GMTADKRGEA VLAAVVGYFV LIKAMGVLLV DVGEYAADAA IVSRLPGNPL IGIIAGLVTA
ALYSRFSNLR LPEALGFFSG RRLVPILTSV AMLVVALALV LVWPLVWDGL ASFNEFLAGL
GALGAAVFGF LNRLLLLLGL HHVMNSFFWF NIGEFVTPEG TMVVGDIPRF LAGDPSAGVY
QVGFYPVMMG GLVGAALAMI RAARPENRRK VAGILGSAAL VSFATGITEP LEFSFVFVAP
LLYGVHALLT GVSMYLTVSL GMTHGFGFSA GLIDYVLNFG LAQHPLGLAV VTVAFFVLYF
AVFSVLIRVL NLRTLGRGDA MEDSEAQAAS SAQPLPVAVA GRVGDEFSER AAGMLAALGG
RENVDSVDSC ATRLRLGVRD SSLADEGALM RYGAKGVIRP SERAVQIIIG SDVQFFADAL
AHLLAQPADA DQRVGDAQSS AKAASEPERA AATTGTAGTA AAIELDALLD ALGGADNLDE
IAASAHTRLR VEVKRGAAVD ESALRACGVR GVLLRGECVE LLVGAGAEQH RASLQALRES
ARA
//
