ID K2IVD8_9RHOB Unreviewed; 696 AA.
AC K2IVD8;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=Lipopolysaccharide biosynthesis family protein {ECO:0000313|EMBL:EKE74346.1};
GN ORFNames=B30_01430 {ECO:0000313|EMBL:EKE74346.1};
OS Celeribacter baekdonensis B30.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Celeribacter.
OX NCBI_TaxID=1208323 {ECO:0000313|EMBL:EKE74346.1, ECO:0000313|Proteomes:UP000006762};
RN [1] {ECO:0000313|EMBL:EKE74346.1, ECO:0000313|Proteomes:UP000006762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B30 {ECO:0000313|EMBL:EKE74346.1,
RC ECO:0000313|Proteomes:UP000006762};
RA Wang W.;
RT "Celeribacter baekdonensis B30 Genome Sequencing.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00001074};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the etk/wzc family.
CC {ECO:0000256|ARBA:ARBA00008883}.
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:EKE74346.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AMRK01000001; EKE74346.1; -; Genomic_DNA.
DR RefSeq; WP_009570192.1; NZ_AMRK01000001.1.
DR AlphaFoldDB; K2IVD8; -.
DR STRING; 1208323.B30_01430; -.
DR PATRIC; fig|1208323.3.peg.295; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR OrthoDB; 230260at2; -.
DR Proteomes; UP000006762; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004713; F:protein tyrosine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0045226; P:extracellular polysaccharide biosynthetic process; IEA:InterPro.
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; IPR032807; GNVR.
DR InterPro; IPR003856; LPS_length_determ_N_term.
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 Pfam; PF13807; GNVR; 1.
DR Pfam; PF02706; Wzz; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000006762};
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};
KW Tyrosine-protein kinase {ECO:0000256|ARBA:ARBA00023137}.
FT TRANSMEM 32..53
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..107
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 357..428
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 508..620
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 209..272
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 317..365
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 696 AA; 76154 MW; 3D2893CE8F855293 CRC64;
MSQNNKPLNT AATDEDVIDL GALFGVLWRK KLWILASIFV FACLGAFYAL GVVTPKYRAT
SVILLDTSGQ QLLDLSAVLP SLGTDSEAIN TEVEVLKSRR LLERVVSVAH LTEDPEFNAA
LRPLSLKDTL KNALTGAEPK DASDQEQITA AINAVLERIS VRNIPNTYIL QVTMETEDAQ
KSATLADTIA EQYILYQMDV KFEATREASE WLTSRVADLK LELEQAEARV AEFSTNSEAV
SIESVQALDR QLKELRDRLT TTRATFNEAE LQLANLVALE SASAQEKAEK AGDARLTTLL
RENGAGAEFD ARFEQLLSRA KTQVQRTEAQ VQSLASSIET REAEIAKQSD EIIQLQQLSR
EAEASRLLYE YFLGRLKETS AQEGIQQADS RILSNAVLPD SPSEPRKSLI LAMSMILGAM
AGSGGALLWE MRQNGYRQAS DLEADTGLSV MGQIPLLPTD NRRQGLEYLA EKPTSAAAEA
VRNLRTSVLL SGLDKAPQVI MSTSSLPGEG KTTVSFALAQ NLVGLGKKVL LVEGDIRRLV
FSQYLDVKDA KGLMSVLAGD VSLEDAVIHD SVLGADILVS EPSNVNAADI LSSRRFIEFL
EAARTAYDFV IIDTPPVLVV PDARVVAQQV DVVLFTVHWD RTTKSQVRDA LRMFETVGVT
ISGIVLNQID PKGMKRYGYG DSYGAYGSYG NKYYTN
//