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Database: UniProt
Entry: F6CRM4_MARPP
LinkDB: F6CRM4_MARPP
Original site: F6CRM4_MARPP 
ID   F6CRM4_MARPP            Unreviewed;       715 AA.
AC   F6CRM4;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
DE   SubName: Full=Capsular exopolysaccharide family {ECO:0000313|EMBL:AEF53787.1};
GN   OrderedLocusNames=Mar181_0731 {ECO:0000313|EMBL:AEF53787.1};
OS   Marinomonas posidonica (strain CECT 7376 / NCIMB 14433 / IVIA-Po-181).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Oceanospirillaceae; Marinomonas.
OX   NCBI_TaxID=491952 {ECO:0000313|EMBL:AEF53787.1, ECO:0000313|Proteomes:UP000009230};
RN   [1] {ECO:0000313|EMBL:AEF53787.1, ECO:0000313|Proteomes:UP000009230}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT 7376 / NCIMB 14433 / IVIA-Po-181
RC   {ECO:0000313|Proteomes:UP000009230};
RX   PubMed=23458837; DOI=10.4056/sigs.2976373;
RA   Lucas-Elio P., Goodwin L., Woyke T., Pitluck S., Nolan M., Kyrpides N.C.,
RA   Detter J.C., Copeland A., Lu M., Bruce D., Detter C., Tapia R., Han S.,
RA   Land M.L., Ivanova N., Mikhailova N., Johnston A.W., Sanchez-Amat A.;
RT   "Complete genome sequence of Marinomonas posidonica type strain (IVIA-Po-
RT   181(T)).";
RL   Stand. Genomic Sci. 7:31-43(2012).
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; CP002771; AEF53787.1; -; Genomic_DNA.
DR   RefSeq; WP_013795264.1; NC_015559.1.
DR   AlphaFoldDB; F6CRM4; -.
DR   STRING; 491952.Mar181_0731; -.
DR   KEGG; mpc:Mar181_0731; -.
DR   eggNOG; COG0489; Bacteria.
DR   eggNOG; COG3206; Bacteria.
DR   HOGENOM; CLU_009912_2_1_6; -.
DR   OrthoDB; 9775724at2; -.
DR   Proteomes; UP000009230; Chromosome.
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; 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; 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   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        25..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        444..464
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          9..99
FT                   /note="Polysaccharide chain length determinant N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02706"
FT   DOMAIN          526..684
FT                   /note="AAA"
FT                   /evidence="ECO:0000259|Pfam:PF13614"
FT   COILED          324..383
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   715 AA;  81832 MW;  2C3DA62993505C4D CRC64;
     MREQGINNDE INLLEIFSII NNKKWMFFIL ILITSFISSY IYYETPETYT SSVNIQVNLN
     KKNGGSILDE LSFGVGRSNS FGSELELIKS RNLLSNVVDV LKLNKDILEE KQKNHIPDYI
     KTTLSSINSV LSKFNKSISI NEIKEDYIEI RTTKKLQGML SISYSESGGF ITISITSYNA
     ELSKNIVNTI ANTYIQYKDR EVDLSEEKTL NWLSGELRNI KNDILRSESE LKSLSGSNDS
     PNIKIMMGLK EDELNTLSHD IKRLKEKLNI EEVYFKKIKE TKDTNIILDS PLINTTNEIE
     RTKGLISSSE TKLLEASFKY GPKHPNYKIL NKNLENEKNK LKTQIENQLN IKKSIFEVEK
     KKLKTLQQSL TEIKLELKKL NQSEDIYLDK LREVESYRNL YNMTLKRFQE SQSISKIKSE
     VARVLDYALL IDVKKNNNRY IKSMLTLLVG GIISLFFSLL LGLLDQKIYN KSSLENITNL
     AVLTALPKTP SSLNTSDSFQ FSTDKIYLES LYRLRTQLRS IHKDKKIISI ASTNAKEGKS
     TTALHLAKAL SEVEKTLLID IDFRRQSITS ILNIPKGKPG LSDIIMKKSK FSQAITKNYK
     EGFDVLGVGN FLDHPNYLLS SPMMKQSLDH LSKYYDRIII ETPPAQIFSD AESVSKLSDG
     LIIIVKSGHT RKKELIEIIN NFEMLKVDIL GTILTKINFS SQKKHYNKYI QEKIA
//
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