ID U2IJB3_9STRE Unreviewed; 579 AA.
AC U2IJB3;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=HMPREF1557_01969 {ECO:0000313|EMBL:ERJ73981.1};
OS Streptococcus sobrinus W1703.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=1227275 {ECO:0000313|EMBL:ERJ73981.1, ECO:0000313|Proteomes:UP000016617};
RN [1] {ECO:0000313|EMBL:ERJ73981.1, ECO:0000313|Proteomes:UP000016617}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W1703 {ECO:0000313|EMBL:ERJ73981.1,
RC ECO:0000313|Proteomes:UP000016617};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ERJ73981.1}.
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DR EMBL; AWVA01000117; ERJ73981.1; -; Genomic_DNA.
DR AlphaFoldDB; U2IJB3; -.
DR PATRIC; fig|1227275.3.peg.1769; -.
DR HOGENOM; CLU_020473_3_3_9; -.
DR Proteomes; UP000016617; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0071555; P:cell wall organization; IEA:InterPro.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR010559; Sig_transdc_His_kin_internal.
DR InterPro; IPR011620; Sig_transdc_His_kinase_LytS_TM.
DR PANTHER; PTHR34220; SENSOR HISTIDINE KINASE YPDA; 1.
DR PANTHER; PTHR34220:SF7; SENSOR HISTIDINE KINASE YPDA; 1.
DR Pfam; PF07694; 5TM-5TMR_LYT; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF06580; His_kinase; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 36..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 84..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 111..130
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 150..169
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 462..569
FT /note="Histidine kinase/HSP90-like ATPase"
FT /evidence="ECO:0000259|SMART:SM00387"
SQ SEQUENCE 579 AA; 64284 MW; D75090FFD85F60C1 CRC64;
MILLFQRLGI IMILAFLLVN NGYFRQLIVE RSKREKLALI IIFGIFVIIS NLTGIEIRGD
KSLIEHPILT TISHSDSLAN TRTLVITTAS LVGGPLVGTI VGIIGGIHRF FQGNFSGLFY
IFSSALVGYV SGRLGDYFKG IKLYPSTSKI ILISLIAESI QMIFVGYFSG WDLVKLIIIP
MMLLNSLGST IFLTILKTYL SNESQLKAVQ TRDVLDLTRE TLPYLRQGLN QFSAAKVCDI
IKQHTNFDAV GLTDHANVLA HIGVGQDHHI SGQPVKTDLS KNVIQTGRPQ VALDRLAISC
PEPGCLLNSA VVVPLKINDQ TIGALKMYFA GDKKMTEVEE NLAIGLAQIF SGQLAIGIAE
EQNKLANMAE IKVLQAQINP HFFFNAINTI SALLRINADK ARYALMQLST FFRTSLQGGQ
EREVTLEQEK SHVDAYMNLE KLRFPDKYQL DYQISVSEKI KLPPFGLQVL VENAVRHAFK
DRKKDNKICI QVKQENDVYR VSVSDNGQGI SPQIIDKLGQ EIVSESTGSG TALVNLNNRL
NLLYGSISHL HFDCDDNGTT VWYLIPQQIG ESEHENFDS
//
