ID A0A3E2XK58_9FIRM Unreviewed; 1112 AA.
AC A0A3E2XK58;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=DW747_11545 {ECO:0000313|EMBL:RGC45488.1};
OS Coprococcus catus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=116085 {ECO:0000313|EMBL:RGC45488.1, ECO:0000313|Proteomes:UP000261231};
RN [1] {ECO:0000313|EMBL:RGC45488.1, ECO:0000313|Proteomes:UP000261231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM28-39 {ECO:0000313|EMBL:RGC45488.1,
RC ECO:0000313|Proteomes:UP000261231};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) 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: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:RGC45488.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QVFD01000011; RGC45488.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2XK58; -.
DR OrthoDB; 9804955at2; -.
DR Proteomes; UP000261231; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd01610; PAP2_like; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.20.144.10; Phosphatidic acid phosphatase type 2/haloperoxidase; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR000160; GGDEF_dom.
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; IPR029787; Nucleotide_cyclase.
DR InterPro; IPR036938; P_Acid_Pase_2/haloperoxi_sf.
DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase.
DR InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF01569; PAP2; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF48317; Acid phosphatase/Vanadium-dependent haloperoxidase; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000261231};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 7..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 32..55
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 288..421
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT DOMAIN 744..969
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 989..1110
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 707..734
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1041
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1112 AA; 126514 MW; C2E1F0377433A66B CRC64;
MGEKKLWKPV LVLACLIGIS RLYLYVHYPT DVLGGVLAGA ISGYLGYRFI QAIFLQNKTR
RGRTMSEVKN KKKKSSMIQV SIGVLAVILA ILIIIMMGIV SDIQGTARIV NYTGLVRGET
QRIIKLEVAG EQDDAMIQEV RSFIDGLRNG NTKLNLVYLN DTDFQNKMQE LDEGFSDLYK
EICLGRSEGY EKTDIISRSE DFFVICDEAT GLAEKYSQKK ATSLSLLEKY ITADIVVLML
LIGYEFIKAI QYAAMNRLLQ RKVYLDDATG LPNKNKCEEL LSEEETDADT GVCSFDLNNL
RRINDSRGHE AGDAYIRRFA ICLRASIPAE QFVGRAGGDE FLVVTHGLDR EQMTQCLEKV
RRDMAEESRV YPDTQLSYAV GFALACDFPG STMRELFNCA DKNMYINKNH VKREEAAAEK
NQGYQLLKLL NQHGSNFSDC LYCDARMDTY RAIRSSENFF LASDGAYSGA VEQIIEEQIE
KSCQADIREG LQISELQKKM HTKKDVLEYE YNIGKQEAYN RLTLIPVDWD EDKRLHHFLL
AFETIRKTSE GQTGAKEQLQ LYYEQLKQSI LENDSYVDAL LELSDVIYTV NLTKDVLERR
IVLNGKEQKS RELFMDYPLP CSYQDYCWEY EKKITQETIA GYCMTDNCEK LRKRFENGET
NMSVEYCARE DDGSIRWVQK TVLMTRMVVF DTEILAEIPM IYAIILLQDT TQRHERDEQE
QARLQAAFNE MRAESRAKTN FLSRMSHDIR TPLNGIIGLL KIDETHFEDK ALIRENHKKM
KIAADYLLSL INDVLQMSKI EEGHIVLTHE YICLKDLVYE IESIITHRAA DEDIQWIYEK
NKEDIPYPYV YGSSLHLRQI FLNIYGNCIK YNRPGGKITT VMEVVDVHDG ICTYRWTISD
TGIGMSAEFL SRIFDPFSQE KTDARSVYQG TGLGMAIARG LIEQMHGSIE VTSQVGVGSV
FVITIPFEIA EKQKKDEEIA EKYNIRGLHL LAAEDNELNA EIIEMLLTDD GAKVTVAKNG
RQAVEYFESN PPGTFDAILM DVLMPVMDGI AATKAIRAMD RADAKTIPII AMTANAFEED
AKRCLAAGMT AHLAKPFQIE DVEKTIVECC GK
//
