ID F9TAH7_9VIBR Unreviewed; 729 AA.
AC F9TAH7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 75.
DE RecName: Full=Ammonium transporter {ECO:0000256|RuleBase:RU362002};
GN ORFNames=IX91_13595 {ECO:0000313|EMBL:AIW15180.1};
OS Vibrio tubiashii ATCC 19109.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio; Vibrio oreintalis group.
OX NCBI_TaxID=1051646 {ECO:0000313|EMBL:AIW15180.1, ECO:0000313|Proteomes:UP000030071};
RN [1] {ECO:0000313|EMBL:AIW15180.1, ECO:0000313|Proteomes:UP000030071}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19109 {ECO:0000313|EMBL:AIW15180.1,
RC ECO:0000313|Proteomes:UP000030071};
RA Richards G.P., Needleman D.S., Watson M.A., Bono J.L.;
RT "First Complete Genome Sequence of the Shellfish Pathogen Vibrio
RT tubiashii.";
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362002};
CC Multi-pass membrane protein {ECO:0000256|RuleBase:RU362002}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ammonia transporter channel (TC 1.A.11.2)
CC family. {ECO:0000256|ARBA:ARBA00005887, ECO:0000256|RuleBase:RU362002}.
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DR EMBL; CP009354; AIW15180.1; -; Genomic_DNA.
DR RefSeq; WP_004747148.1; NZ_CP009354.1.
DR AlphaFoldDB; F9TAH7; -.
DR STRING; 1051646.IX91_13595; -.
DR KEGG; vtu:IX91_13595; -.
DR PATRIC; fig|1051646.9.peg.2669; -.
DR eggNOG; COG0004; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_33_6_6; -.
DR Proteomes; UP000030071; Chromosome 1.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00075; HATPase; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.3430.10; Ammonium transporter AmtB like domains; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR029020; Ammonium/urea_transptr.
DR InterPro; IPR001905; Ammonium_transpt.
DR InterPro; IPR018047; Ammonium_transpt_CS.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00836; amt; 1.
DR PANTHER; PTHR11730; AMMONIUM TRANSPORTER; 1.
DR PANTHER; PTHR11730:SF6; AMMONIUM TRANSPORTER; 1.
DR Pfam; PF00909; Ammonium_transp; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF111352; Ammonium transporter; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS01219; AMMONIUM_TRANSP; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 3: Inferred from homology;
KW Ammonia transport {ECO:0000256|ARBA:ARBA00023177,
KW ECO:0000256|RuleBase:RU362002}; Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362002};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362002};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362002};
KW Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU362002}.
FT TRANSMEM 5..23
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 44..64
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 84..106
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 113..134
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 186..204
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 216..237
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 249..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 274..292
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 304..326
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT TRANSMEM 338..361
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362002"
FT DOMAIN 405..439
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 522..727
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 729 AA; 79246 MW; 749F3FFA06E5807C CRC64;
MDPLFILLCT LLVLLMQVGF LFLEAGTVRK KNTANVAAKN LIDLAVVLIL YWLVGYGVMF
GESMDGYLGT SHFLLGHFEG LDDGAFFVFQ MVFCATSVTI ISGAIAERGS LKGYIALSVF
VAAVIYPVIG HWVWSDNGWL AQRGFIDFAG STVVHSVGGW AALAAIMIIG PRLNRFVEGH
NFNHSSLVQS VAGVVFLWIG WLGFNAGSSL HFDSNVFNIV LNTILAGAAG GLTSAMYSLH
KTNRVHIPNF YNGILSGLVS ITASCNFVDG LSSVLIGSLG ALISLSVGRL LVMKKIDDVV
DAVPVHLASG TWGTIALALF IPQSVITDTL LMSDRMELLW SQVFGVSVVA AFVFPLCYLV
FSLINKVLPL RVGQEEEIVG LNISSHQASS DLYDLVTVMQ NQEESGDFSQ RVDYDPTSEI
GMIARQYNRV LSRFETALVK ATQKHSALLQ TNQRLKSMES RVQKSEKLSS LGQISSGLVR
EINEPIGYVL SNIKTLKDYN KFFKLLVTEY KAFAATVSQH PVVANEVLQR IDKICEEEDL
EFVLEDSEEL INATSDGASK IEKILSNVRT FSEFGDEKFE LKDINVLVSA AVEKVAATLP
LSCKLLESYE AKLPMVSCSP HQIEQLCINV LSNSVQAIGE DRGAIKITTS NEGNQVVVAI
IDSGVGIKEE HQAKVFEPFF TTFGTQGHAG LGLSICYGIA TNHGGSLSLL SKQAKGTKVT
LRLPMPLDE
//