KINB_PSEAI
ID KINB_PSEAI Reviewed; 595 AA.
AC O34206;
DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 127.
DE RecName: Full=Alginate biosynthesis sensor protein KinB {ECO:0000305};
DE EC=2.7.13.3 {ECO:0000269|PubMed:9218420};
GN Name=kinB;
OS Pseudomonas aeruginosa.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP SUBCELLULAR LOCATION, TOPOLOGY, PHOSPHORYLATION AT HIS-385, AND MUTAGENESIS
RP OF HIS-385; ASN-504; ASP-532 AND GLY-560.
RC STRAIN=FRD444;
RX PubMed=9218420; DOI=10.1074/jbc.272.29.17952;
RA Ma S., Wozniak D.J., Ohman D.E.;
RT "Identification of the histidine protein kinase kinB in Pseudomonas
RT aeruginosa and its phosphorylation of the alginate regulator algB.";
RL J. Biol. Chem. 272:17952-17960(1997).
CC -!- FUNCTION: Member of the two-component regulatory system AlgB/KinB
CC involved in regulation of alginate biosynthesis genes. KinB functions
CC as a membrane-associated protein kinase that phosphorylates AlgB,
CC probably in response to environmental signals.
CC {ECO:0000269|PubMed:9218420}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000269|PubMed:9218420};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:9218420};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- PTM: Autophosphorylated. {ECO:0000269|PubMed:9218420}.
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DR EMBL; U97063; AAB68790.1; -; Genomic_DNA.
DR PDB; 3KKB; X-ray; 1.88 A; A/B=41-168.
DR PDBsum; 3KKB; -.
DR AlphaFoldDB; O34206; -.
DR SMR; O34206; -.
DR iPTMnet; O34206; -.
DR PRIDE; O34206; -.
DR eggNOG; COG5002; Bacteria.
DR BRENDA; 2.7.13.3; 5087.
DR EvolutionaryTrace; O34206; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0042121; P:alginic acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR Gene3D; 1.20.120.880; -; 1.
DR Gene3D; 3.30.565.10; -; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR038320; KinB_N_sf.
DR InterPro; IPR031909; KinB_sensor_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF16767; KinB_sensor; 1.
DR Pfam; PF08448; PAS_4; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00091; PAS; 1.
DR SUPFAM; SSF47384; SSF47384; 1.
DR SUPFAM; SSF55785; SSF55785; 1.
DR SUPFAM; SSF55874; SSF55874; 1.
DR TIGRFAMs; TIGR00229; sensory_box; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alginate biosynthesis; ATP-binding; Cell inner membrane;
KW Cell membrane; Kinase; Membrane; Nucleotide-binding; Phosphoprotein;
KW Sensory transduction; Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..595
FT /note="Alginate biosynthesis sensor protein KinB"
FT /id="PRO_0000074778"
FT TOPO_DOM 1..12
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9218420"
FT TRANSMEM 13..33
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 34..167
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:9218420"
FT TRANSMEM 168..188
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 189..595
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9218420"
FT DOMAIN 195..247
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 258..323
FT /note="PAS"
FT /evidence="ECO:0000305"
FT DOMAIN 327..369
FT /note="PAC"
FT /evidence="ECO:0000305"
FT DOMAIN 382..595
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 385
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107,
FT ECO:0000269|PubMed:9218420"
FT MUTAGEN 385
FT /note="H->K,Q: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:9218420"
FT MUTAGEN 504
FT /note="N->Q: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:9218420"
FT MUTAGEN 532
FT /note="D->E: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:9218420"
FT MUTAGEN 532
FT /note="D->N: Residual autophosphorylation."
FT /evidence="ECO:0000269|PubMed:9218420"
FT MUTAGEN 560
FT /note="G->A: Loss of autophosphorylation."
FT /evidence="ECO:0000269|PubMed:9218420"
FT HELIX 42..70
FT /evidence="ECO:0007829|PDB:3KKB"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:3KKB"
FT HELIX 77..97
FT /evidence="ECO:0007829|PDB:3KKB"
FT HELIX 101..118
FT /evidence="ECO:0007829|PDB:3KKB"
FT HELIX 121..126
FT /evidence="ECO:0007829|PDB:3KKB"
FT STRAND 131..133
FT /evidence="ECO:0007829|PDB:3KKB"
FT HELIX 134..162
FT /evidence="ECO:0007829|PDB:3KKB"
SQ SEQUENCE 595 AA; 66072 MW; BA12FC7E3120F048 CRC64;
MSMPLPMKLR TRLFLSISAL ITVSLFGLLL GLFSVMQLGR AQEQRMSHHY ATIEVSQQLR
QLLGDQLVIL LRETPDGQAL ERSQNDFRRV LEQGRANTVD SAEQAALDGV RDAYLQLQAH
TPALLEAPMV DNDGFSEAFN GLRLRLQDLQ QLALAGISDA ETSARHRAYL VAGLLGLVGV
AILLIGFVTA HSIARRFGAP IETLARAADR IGEGDFDVTL PMTNVAEVGQ LTRRFGLMAE
ALRQYRKTSV EEVLSGERRL QAVLDSIDDG LVIFDNQGRI EHANPVAIRQ LFVSNDPHGK
RIDEILSDVD VQEAVEKALL GEVQDEAMPD LVVDVAGESR LLAWSLYPVT HPGGHSVGAV
LVVRDVTEQR AFERVRSEFV LRASHELRTP VTGMQMAFSL LRERLDFPAE SREADLIQTV
DEEMSRLVLL INDLLNFSRY QTGMQKLELA SCDLVDLLTQ AQQRFIPKGE ARRVSLQLEL
GDELPRLQLD RLQIERVIDN LLENALRHSS EGGQIHLQAR RQGDRVLIAV EDNGEGIPFS
QQGRIFEPFV QVGRKKGGAG LGLELCKEII QLHGGRIAVR SQPGQGARFY MLLPV
