ID Q58Z27_LACRH Unreviewed; 250 AA.
AC Q58Z27;
DT 26-APR-2005, integrated into UniProtKB/TrEMBL.
DT 26-APR-2005, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Tyrosine-protein kinase CpsD {ECO:0000256|ARBA:ARBA00019200};
DE EC=2.7.10.2 {ECO:0000256|ARBA:ARBA00011903};
GN Name=wze {ECO:0000313|EMBL:AAW22470.1};
OS Lacticaseibacillus rhamnosus (Lactobacillus rhamnosus).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=47715 {ECO:0000313|EMBL:AAW22470.1};
RN [1] {ECO:0000313|EMBL:AAW22470.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R {ECO:0000313|EMBL:AAW22470.1};
RA Provencher C., Sirois S., Lapointe G., Roy D.;
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AAW22470.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=R {ECO:0000313|EMBL:AAW22470.1};
RX PubMed=15941992; DOI=10.1099/mic.0.27852-0;
RA Peant B., Lapointe G., Gilbert C., Atlan D., Ward P., Roy D.;
RT "Comparative analysis of the exopolysaccharide biosynthesis gene clusters
RT from four strains of Lactobacillus rhamnosus.";
RL Microbiology 151:1839-1851(2005).
CC -!- FUNCTION: Involved in the regulation of capsular polysaccharide
CC biosynthesis. Autophosphorylation of CpsD attenuates its activity and
CC reduces the level of encapsulation. May be part of a complex that
CC directs the coordinated polymerization and export to the cell surface
CC of the capsular polysaccharide. {ECO:0000256|ARBA:ARBA00024964}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001149};
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005132}.
CC -!- SIMILARITY: Belongs to the CpsD/CapB family.
CC {ECO:0000256|ARBA:ARBA00007316}.
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DR EMBL; AY659978; AAW22470.1; -; Genomic_DNA.
DR RefSeq; WP_070786841.1; NZ_RINB01000030.1.
DR AlphaFoldDB; Q58Z27; -.
DR UniPathway; UPA00934; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd05387; BY-kinase; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR025669; AAA_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR005702; Wzc-like_C.
DR NCBIfam; TIGR01007; eps_fam; 1.
DR PANTHER; PTHR32309; TYROSINE-PROTEIN KINASE; 1.
DR PANTHER; PTHR32309:SF13; TYROSINE-PROTEIN KINASE ETK-RELATED; 1.
DR Pfam; PF13614; AAA_31; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Capsule biogenesis/degradation {ECO:0000256|ARBA:ARBA00022903};
KW Exopolysaccharide synthesis {ECO:0000256|ARBA:ARBA00023169};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT DOMAIN 69..210
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 250 AA; 27414 MW; 340A531D3E424B86 CRC64;
MNFSLEKVLH RHKEDQETQK NGVMLVTFAE PKHVVSEQFR TVRTNIEFAG AALDQCQVIM
FTSSAMFEGK PTVSANVAVT WAQAGKKVLL IDADLRRPTV HATFRTLNLD GVTTVLTGKE
KPDDVVEETF VDNMSIITSG PVPPNPSELL NSKRMAGLLE WAREKYDIIV LDAPPVLAVS
DVQVLVPKTD GVVVVANMGK TLKGDLKRTV EVLKLANAKI LGSVERVKAK HGDRGYGYGY
GYGYGNESNK
//