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Database: UniProt
Entry: A0A1N6HR42_9SPHN
LinkDB: A0A1N6HR42_9SPHN
Original site: A0A1N6HR42_9SPHN 
ID   A0A1N6HR42_9SPHN        Unreviewed;       735 AA.
AC   A0A1N6HR42;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:SIO22149.1};
GN   ORFNames=SAMN02745824_3412 {ECO:0000313|EMBL:SIO22149.1};
OS   Parasphingorhabdus marina DSM 22363.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Parasphingorhabdus.
OX   NCBI_TaxID=1123272 {ECO:0000313|EMBL:SIO22149.1, ECO:0000313|Proteomes:UP000185192};
RN   [1] {ECO:0000313|Proteomes:UP000185192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22363 {ECO:0000313|Proteomes:UP000185192};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) 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; FSQW01000002; SIO22149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1N6HR42; -.
DR   STRING; 1123272.SAMN02745824_3412; -.
DR   Proteomes; UP000185192; 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:UP000185192};
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        44..68
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          32..119
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          401..470
FT                   /note="Tyrosine kinase G-rich"
FT                   /evidence="ECO:0000259|Pfam:PF13807"
FT   DOMAIN          548..697
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          213..247
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          338..387
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        1..17
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   735 AA;  81265 MW;  100EB3751C3D08E5 CRC64;
     MVVEAKNTTS PHNMNQVDVN SDDRRDEQVP LLLQYWQAVS RYRIGIACIV LGTIALGIIV
     TLLMTPYYTA TSRIEINRNQ DKVTNVEGLE AEDVGQNLEF YQTQYALLEA RSLADRVVRS
     ENLATGDAFF QTFNVDPDEN GIISGSDSRQ SSEDRRRRFE LAIRLLLDNV SISPVRGSSL
     VDVSFRSPDP QLSASIANAW VAQFVDSNLD RRFDSTIDAR KFLEERLAQL RARLEDSERR
     LVRYADNKEI VTLSTTRDAE GSTVGGDTLI SSNLAALNKA LTDATADRIA AQAQADQNGL
     NKDAIENPAI NGMRQKRAEI ASEYAKILVQ FEPEYPTAKA LERQISDLDE SIEKEELRMR
     TGALTRYSEA LKRERNLQNQ VAQLKSKFSG ERQDTIQYNI FQREVDTNRQ LYNGLLQRYK
     EIGVAGVGSN NIAVVDPALA PEQPSSPRIL LNMALAMLMG LGLAGAYVVV SEQIDQTIKD
     PSDLKNRLNL APLGSVPDMR KDDIISMLQD KKSVAWEAYI SIQTSLSFLT SHGAPRSFLM
     TSTRPNEGKS TSAFALAAVL SSTNRKVLLI DGDMRNPSLH QMIDQKNVQG LSNYLSGDDD
     IDNLIQKMPD QGFWVMTAGP IPPNAAELLS SPRIKKLFDH LEEKFDCVIV DAPPVLGLAD
     IPLLANAVEG VIYTIEAGGV KVRGIESALR RVRSSHATIF GAIITKVKSS GTGYGYGYDY
     QYSYGQQDPL PAPSA
//
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