ID A0A0F4Q6N7_9GAMM Unreviewed; 737 AA.
AC A0A0F4Q6N7;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=Chain-length determining protein {ECO:0000313|EMBL:KJZ02227.1};
GN ORFNames=TW72_00690 {ECO:0000313|EMBL:KJZ02227.1};
OS Pseudoalteromonas ruthenica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=151081 {ECO:0000313|EMBL:KJZ02227.1, ECO:0000313|Proteomes:UP000033664};
RN [1] {ECO:0000313|EMBL:KJZ02227.1, ECO:0000313|Proteomes:UP000033664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S3137 {ECO:0000313|EMBL:KJZ02227.1,
RC ECO:0000313|Proteomes:UP000033664};
RX PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT bacteria.";
RL BMC Genomics 16:158-158(2015).
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:KJZ02227.1}.
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DR EMBL; JXXZ01000001; KJZ02227.1; -; Genomic_DNA.
DR RefSeq; WP_045978971.1; NZ_PNCF01000014.1.
DR AlphaFoldDB; A0A0F4Q6N7; -.
DR GeneID; 58227001; -.
DR PATRIC; fig|151081.8.peg.1320; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR OrthoDB; 9775724at2; -.
DR Proteomes; UP000033664; 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:UP000033664};
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 26..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 449..468
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 16..104
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 394..468
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 539..680
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT COILED 223..280
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 357..391
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 737 AA; 82966 MW; F773A0ABC60258F7 CRC64;
MKTATRNTGA AEVVTLGYYL KVINKFKWRI ALLAILVTTL AMVWALQLTP SYRASATLLI
EAQQRKAVSF EEVYGLDASK KEYYQTQYEI LRSRAIARDV IEQLNLLEHR DFQPKPSMLS
WVMNDIKQWV KQYIPQKPQT LPSTADAQQA YEKRMQKIIT AFSRRLSIHP IRKTQLVVIA
YESSDPALAA DVANAVGEAY ITHAMQAKMG IAKQASGWLN DRLSILRERL DKSEQKLQSY
REREDLVDIE GVVGLVRREL EQTAQQLVEA KRNQSELNAI MRVVDEYGRD DIARLESINE
ITTHKVIQDV KREVVTAQRK VSELRQVYGP KHPKMIAARA ELATVQENLS AQIRSLVMGL
EKEMRTANST VSALQQDVEQ LRQRFQMLTR KETEYHQLKR EVETNRNIYD TFLSRSKETE
VTSDFNSPIA RFTDYAYQPT NPAKPNRKLI VVLAFVATLG FGIVLAFLTD ALNDTLNNAE
EVENKLGQRL LGVLPSLPSS KRKPLPTHTF FDKGKLAFAE AVRTFRTSLV LSQMDRDNQV
IEVTSSVPGE GKSTTSINLA FSLGQMEKVL LIDADMRRPS LAGRFSLPAY QPGLANVLAN
TQQLEECIHV DEQSNIHVLC AGQIPSNPLE LLSSENFKAL LAHLRQQYDY IVLDTAPLEA
VSDALVVSQH SDSVIYVVKS GSTRQGLVKA GLHRLIDAKA NICGVLLNQV NGKQKQGHNA
HYGYYDSHGY TQANAPT
//
