ID B4S3Z6_PROA2 Unreviewed; 803 AA.
AC B4S3Z6;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 86.
DE SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:ACF46788.1};
DE EC=2.7.10.2 {ECO:0000313|EMBL:ACF46788.1};
GN OrderedLocusNames=Paes_1775 {ECO:0000313|EMBL:ACF46788.1};
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512 {ECO:0000313|EMBL:ACF46788.1, ECO:0000313|Proteomes:UP000002725};
RN [1] {ECO:0000313|EMBL:ACF46788.1, ECO:0000313|Proteomes:UP000002725}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413 {ECO:0000313|Proteomes:UP000002725};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
RL Submitted (JUN-2008) 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}.
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DR EMBL; CP001108; ACF46788.1; -; Genomic_DNA.
DR RefSeq; WP_012506321.1; NC_011059.1.
DR AlphaFoldDB; B4S3Z6; -.
DR STRING; 290512.Paes_1775; -.
DR KEGG; paa:Paes_1775; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_2_1_10; -.
DR Proteomes; UP000002725; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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: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:UP000002725};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACF46788.1};
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 27..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..102
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 405..484
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 608..740
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
FT REGION 539..558
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 208..272
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 408..435
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 541..555
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 90336 MW; 2BDE3D8A790E0840 CRC64;
MTNNDPNQFE QEINIQELLQ VLWNNKLIIG AVTGLVVMLV LLYHFSATPE YRSTSMVLIK
QDKGGAMGEM INPFGSLTGF DLQNDIELVK SFPLAEEVVR NLYTKKDRDT LQLFGERNYV
SPIGGLFGWL SFGGAAEKDS VDYDVQMRKY AAALQERIKV GNSRDTDILN VSVSSPFPEE
AALLTNAICQ AYMRKDIEWN ADQAMSVKEF VGEQLAQQQR EISSVENKLS SYMKNQNIYE
LTGNAEKLLE KLVEAESRYN DAQAEYNILK KRQDFLVQKL SDEEKQISAR IAKNVDQQSI
DLKSRIKKEE KALIELANST GTEDGSYIAK KQQLDVLKQR LQELTRNMIA GELSYTSRAR
QFQFDLISEQ LQTDLRMAEL GYVAQEYLRA KNYYESQLNR LPQKQLNYAR LQRDREVLNN
TYTFLKEKLE ESRIKIASEV GKVVIVGAAY PELAPVAPSL KKNLLIGLIL GLGLGGALVF
VREMLDHSLK DDSFLEDHGF TPLAAIPFVD SDGGGSMQAS MKKSLKDFAS VFPFLSGNTD
GKKDQHQKKN SYGKPVESTR NKQPLLIADS LSSAFAESFR DLRTNITFSQ ADRTLKSILV
TGTEISEGKS TVCTNLAFAF ALTGKKVLIV DCDLRRPSQH RNLNTMRMPG LSDYLAGQEK
DINAVLQPTM HENLSVLPAG SQTPSPNELL GSNKMTELVK KLEEEWDYVI LDTPPVLLLS
DATLLSRTAD GILMVVRMGY TNKNLLKEVQ KLDYLKHRLL GVAIIGPSDK SGYSNYGRYY
GRYGYKGYYS YKSYNAYLEP EKG
//
