ID A0A371IKN7_9FIRM Unreviewed; 512 AA.
AC A0A371IKN7;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 14.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=BBG48_007000 {ECO:0000313|EMBL:RDY21020.1};
OS Criibacterium bergeronii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Criibacterium.
OX NCBI_TaxID=1871336 {ECO:0000313|EMBL:RDY21020.1, ECO:0000313|Proteomes:UP000093352};
RN [1] {ECO:0000313|EMBL:RDY21020.1, ECO:0000313|Proteomes:UP000093352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCRI-22567 {ECO:0000313|EMBL:RDY21020.1,
RC ECO:0000313|Proteomes:UP000093352};
RX PubMed=27587833;
RA Maheux A.F., Berube E., Boudreau D.K., Raymond F., Corbeil J., Roy P.H.,
RA Boissinot M., Omar R.F.;
RT "Draft Genome Sequence of Criibacterium bergeronii gen. nov., sp. nov.,
RT Strain CCRI-22567T, Isolated from a Vaginal Sample from a Woman with
RT Bacterial Vaginosis.";
RL Genome Announc. 4:e00959-16(2016).
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 -!- 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:RDY21020.1}.
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DR EMBL; MBEW02000014; RDY21020.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A371IKN7; -.
DR STRING; 1871336.BBG48_09270; -.
DR Proteomes; UP000093352; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF08447; PAS_3; 2.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00283; MA; 1.
DR SMART; SM00086; PAC; 2.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50113; PAC; 2.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000093352};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284}.
FT DOMAIN 159..211
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 298..350
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 350..512
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 512 AA; 57879 MW; 201D81C02AE3F649 CRC64;
MKLCFHKTKL GEGTMFGKNK LTEKPSDNDF DKQIDNIIAG YNHNEKIQHI QAGSNAQLEN
KINSLIDLFN QELDYQKLRL KVVNDAAHSG MWYMKIDDNL NIEYAIWSDE FRRMTGFKDE
RDFPNEVNSW SDRLHPDDAG NTLEKFGNCI SDFSGKTVYD VNYRLKIKDG TYKWFKATGH
TIRDEKGHPV EIIGIFIDID EQIKNETELD YTVKRYEAID EILSEGSWNM RVTGNDPTSP
NNEFWWSNQF RNLLGYNNES DFPNKLNSWS DKLHPEDKQR TLDAFSKHIL DYSGKTPFDL
DYRLQKKDGR YGWFHAIGQT IRKPNGEPIL VAGAIRDITS EKAKETFTRE LDGLIRDLSG
SIGEITEAVA STTQTTMDIT NKQVEIKKAT EISKAVTDET MKLVDLILNI SSQTNLLALN
ASIEAARAGE AGKGFSVVAE EVRKLANSSQ GAVDSITKSL NGMETANNDI MSRINDISGL
IEGQSSSMQE INASIEEVNS MTTKIADMAQ DL
//
