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Database: UniProt
Entry: F9TAH7_9VIBR
LinkDB: F9TAH7_9VIBR
Original site: F9TAH7_9VIBR 
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
//
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