ID C9MNA4_9BACT Unreviewed; 839 AA.
AC C9MNA4;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Putative phage head-tail adaptor {ECO:0000313|EMBL:EEX19073.1};
GN ORFNames=HMPREF0973_01090 {ECO:0000313|EMBL:EEX19073.1};
OS Prevotella veroralis F0319.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Prevotella.
OX NCBI_TaxID=649761 {ECO:0000313|EMBL:EEX19073.1, ECO:0000313|Proteomes:UP000003327};
RN [1] {ECO:0000313|EMBL:EEX19073.1, ECO:0000313|Proteomes:UP000003327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0319 {ECO:0000313|EMBL:EEX19073.1,
RC ECO:0000313|Proteomes:UP000003327};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (SEP-2009) 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:EEX19073.1}.
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DR EMBL; ACVA01000021; EEX19073.1; -; Genomic_DNA.
DR RefSeq; WP_004382736.1; NZ_GG698712.1.
DR AlphaFoldDB; C9MNA4; -.
DR STRING; 649761.HMPREF0973_01090; -.
DR eggNOG; COG0489; Bacteria.
DR eggNOG; COG3206; Bacteria.
DR HOGENOM; CLU_009912_6_0_10; -.
DR OrthoDB; 9794577at2; -.
DR Proteomes; UP000003327; 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 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:UP000003327};
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 35..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 514..534
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 22..116
FT /note="Polysaccharide chain length determinant N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02706"
FT DOMAIN 457..533
FT /note="Tyrosine kinase G-rich"
FT /evidence="ECO:0000259|Pfam:PF13807"
FT DOMAIN 602..727
FT /note="AAA"
FT /evidence="ECO:0000259|Pfam:PF13614"
SQ SEQUENCE 839 AA; 93565 MW; 6A4683C4871298AE CRC64;
MEETTKLELD KEQEKQGIAS FFDFAALYRT VILNWYWFVL SLIIFGGIGA IYLRYTTPLY
QSTAKLLIKD EDNNSRRGSS LQNMSNLGII SNSTGVDNEM EILSSHSIAE DAIRDLKLYV
NYTTEGKVKD IIAYRDQPLT VDIDAAHLDR LNRPINLNIT KKGSSYIVTG TYSVPTNEEN
IEGPFSINKK FTSLPATIPT RAGIITINSN NGRTLQEAQV LKVNIVSPKM ASDKYVGELQ
IAPSAKGTSI VQLQLTDEVP QRSLDYLKQL AIVYNRQANE DKNVVAHQTE KFINSRLEKI
NAELGKTEGE LQNYKQRNGM VELKMNASNS VTNQNASEQK LAEMETQIEL FNTIAREVES
SSRNLSQVIP SNVGLDDESS TALINKYNEL VLERNRLLRS ASESSPVVEP LTAQIRDLNY
NIRRAIASAR RNLQIQRDAL LTQVDKYTNE VEETPQQERM LTQIGRQQEV KSGLYLMLLQ
KREENSISLA ATADKGKLID DPQLNGQVSP NSTYIMLIAL AIGLTIPVAI ILLIQLFRYK
IEGHDDVARL TKLPIIADIA IASNSAKSKA GIVVHENQNN QMEEIFRALR TNLQFMLHEG
EKVVLFTSST SGEGKTFTAS NLSVSLGLLG KKVILVGLDI RRPRLAEQFG IKDHKHGITN
LLVKDNPNAE DVEAQILPSG VNKNLDLLMA GPVPPNPAEL IARSSLETII AILKDKYDYI
MIDTAPVGLV TDTLQIGRIA NATIYMCRAD YTPKASFGMI NALAMEEKLP NMAMVLNGVD
MSKKKYSYYY GYGKYGKYGR YGYGSGYSYG KYGNYGNYGS YGNYSNSYYG DKNDHSVKR
//
