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Database: UniProt
Entry: K2IVD8_9RHOB
LinkDB: K2IVD8_9RHOB
Original site: K2IVD8_9RHOB 
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}.
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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
//
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