ID A0A1F2PJW2_9FIRM Unreviewed; 1091 AA.
AC A0A1F2PJW2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN Name=barA_2 {ECO:0000313|EMBL:OFV71031.1};
GN ORFNames=ACWI_16170 {ECO:0000313|EMBL:OFV71031.1};
OS Acetobacterium wieringae.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Acetobacterium.
OX NCBI_TaxID=52694 {ECO:0000313|EMBL:OFV71031.1, ECO:0000313|Proteomes:UP000176244};
RN [1] {ECO:0000313|EMBL:OFV71031.1, ECO:0000313|Proteomes:UP000176244}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1911 {ECO:0000313|EMBL:OFV71031.1,
RC ECO:0000313|Proteomes:UP000176244};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Acetobacterium wieringae DSM 1911.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May play the central regulatory role in sporulation. It may
CC be an element of the effector pathway responsible for the activation of
CC sporulation genes in response to nutritional stress. Spo0A may act in
CC concert with spo0H (a sigma factor) to control the expression of some
CC genes that are critical to the sporulation process.
CC {ECO:0000256|ARBA:ARBA00024867}.
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 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 -!- 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:OFV71031.1}.
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DR EMBL; LKEU01000027; OFV71031.1; -; Genomic_DNA.
DR RefSeq; WP_070370925.1; NZ_LKEU01000027.1.
DR AlphaFoldDB; A0A1F2PJW2; -.
DR STRING; 52694.ACWI_16170; -.
DR OrthoDB; 9804263at2; -.
DR Proteomes; UP000176244; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00088; HPT; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.120.160; HPT domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR003661; HisK_dim/P.
DR InterPro; IPR036097; HisK_dim/P_sf.
DR InterPro; IPR036641; HPT_dom_sf.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR008207; Sig_transdc_His_kin_Hpt_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01627; Hpt; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00073; HPT; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50894; HPT; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
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, ECO:0000313|EMBL:OFV71031.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OFV71031.1};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT DOMAIN 357..577
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 595..716
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 742..858
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 914..1012
FT /note="HPt"
FT /evidence="ECO:0000259|PROSITE:PS50894"
FT MOD_RES 649
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 791
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 953
FT /note="Phosphohistidine"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00110"
SQ SEQUENCE 1091 AA; 123653 MW; A8F5C29B8DFF2300 CRC64;
MADQANTGLD QREKIIDQLY LHTELIREIS QMESGINGDI EGFSEEITEL LGNRLEADRV
SIWQYNNEMT MMECLDLYVK KEQTHSKKMT MNRADQPLTF EYLIKNRYMI IDNKSVEPQE
KDYWQAYMKP LGGTTLLVCS ILCNGKAIGS IGFMYVNRKH EWGSDEITFG CHIADQIGTA
FLNRERMAIT QALRKNEAFL NRAQQVSKTG HWHFDIETNC LTWSDETYRI FGVEIGTPQT
FESYMGFVYP DDRKNIIENW TKKSVEGQPF TVLHRIVAGD QIRWVEERSE FEHDQQGNPV
ASWGTVADVT EKMNYLKELE NYQKHLEEMV ISRTTDLEKA KLDAEAANQA KSAFLSNMSH
EIRTPMNAII GLSHLIRRDP LTMRQEEQLD KLTEAANHLL HIINDVLDLS KIEAGKMQLD
AHDFEPTREI DRVCNLLADE AAKKNLNILV DVDHIPTVLQ GDSVRFGQIL LNLMSNAVKF
TEKGSIKIVA RIINQDHKQI RLRFEVCDTG IGMSKNQINK LFQDFVQADE SMTRLYGGTG
LGLAISSRLV NFLGGDIGVH SELGLGSRFW FELPFEKTTA LPKNRINIAS SETMRVLVID
DMQEARELVI SMLADFGIQC DAVNSGNEGL AAVKKADQMT VPYRLVLMDL KMPEMDGIDT
ALMLQSLELK TRPEVYLITG YGNQISAEEA RRAGISRILV KPMTPSTLND ALMELLDDNL
DAQIPSSLND LETRLKHYQP AHILIVEDNQ INQEIVRQLF EPFNFKIELA ENGQEAIDRI
TQKKFDLILM DVQMPVMDGL SATTKIRSLP GWEAVPILAM TANAFEEDRK KCIKAGMNDH
LVKPVEPEIL YKSLIKWLPV RSVQSEHKDK PRSHTEKDLV RQAIVSPDIQ NQLKILRQVD
GLNVETGLRI LGGDASVYLR LIQQFAQKCQ ADTDYIVSQN AAENYPSILQ TVHSIKGVAG
NLGAIKIQEL AADLEQAVRI GSGKAQFEKQ IDNFVNALSS FVEALPKAGY APERIKEGVD
NRDQVNGILS QLAVLLENND TEAYDLFEEH KDQLIPALGN AGFELERQIH EFDYREALET
LRVSFTKQEK V
//
