ID NISK_LACLL Reviewed; 447 AA.
AC P42707;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Nisin biosynthesis sensor protein NisK;
DE EC=2.7.13.3;
GN Name=nisK;
OS Lactococcus lactis subsp. lactis (Streptococcus lactis).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1360;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=6F3;
RX PubMed=8161176; DOI=10.1128/aem.60.3.814-825.1994;
RA Engelke G., Gutowski-Eckel Z., Kiesau P., Siegers K., Hammelmann M.,
RA Entian K.-D.;
RT "Regulation of nisin biosynthesis and immunity in Lactococcus lactis 6F3.";
RL Appl. Environ. Microbiol. 60:814-825(1994).
CC -!- FUNCTION: Member of the two-component regulatory system NisK/NisR
CC involved in the regulation of the biosynthesis of lantibiotic nisin.
CC NisK may function as a membrane-associated protein kinase that
CC phosphorylates NisR in response to environmental signals.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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DR EMBL; X76884; CAA54212.1; -; Genomic_DNA.
DR PIR; S44133; S44133.
DR RefSeq; WP_014570412.1; NZ_ML956318.1.
DR AlphaFoldDB; P42707; -.
DR SMR; P42707; -.
DR BRENDA; 2.7.13.3; 2903.
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 CDD; cd16975; HATPase_SpaK_NisK-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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; IPR008358; Sig_transdc_His_kin/Pase_MprB.
DR InterPro; IPR044082; SpaK_NisK-like_HATPase.
DR PANTHER; PTHR45453; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR PANTHER; PTHR45453:SF1; PHOSPHATE REGULON SENSOR PROTEIN PHOR; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR PRINTS; PR01780; LANTIREGPROT.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cell membrane; Kinase; Membrane; Nucleotide-binding;
KW Phosphoprotein; Transferase; Transmembrane; Transmembrane helix;
KW Two-component regulatory system.
FT CHAIN 1..447
FT /note="Nisin biosynthesis sensor protein NisK"
FT /id="PRO_0000074818"
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 147..167
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 235..447
FT /note="Histidine kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
FT MOD_RES 238
FT /note="Phosphohistidine; by autocatalysis"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00107"
SQ SEQUENCE 447 AA; 51320 MW; 47F10533F5A9685D CRC64;
MGKKYSMRRR IWQAVIEIII GTCLLILLLL GLTFFLRQIG QISGSETIRL SLDSDNLTIS
DIERDMKHYP YDYIIFDNDT SKILGGHYVK SDVPSFVASK QSSHNITEGE ITYTYSSNKH
FSVVLRQNSM PEFTNHTLRS ISYNQFTYLF FFLGEIILII FSVYHLIREF SKNFQAVQKI
ALKMGEITTF PEQEESKIIE FDQVLNNLYS KSKELAFLIE AERHEKHDLS FQVAALSHDV
KTPLTVLKGN IELLEMTEVN EQQADFIESM KNSLTVFDKY FNTMISYTKL LNDENDYKAT
ISLEDFLIDL SVELEELSTT YQVDYQLVKK TDLTTFYGNT LALSRALINI FVNACQYAKE
GEKIVSLSIY DDEKYLYFEI WNNGHPFSEQ AKKNAGKLFF TEDTGRSGKH YGIGLSFAQG
VALKHQGNLI LSNPQKGGAE VILKIKK
//
