ID A0A1B8RQ52_9CLOT Unreviewed; 343 AA.
AC A0A1B8RQ52;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN ORFNames=CP373A1_10390 {ECO:0000313|EMBL:OBY10896.1};
OS Clostridium paraputrificum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=29363 {ECO:0000313|EMBL:OBY10896.1, ECO:0000313|Proteomes:UP000092714};
RN [1] {ECO:0000313|EMBL:OBY10896.1, ECO:0000313|Proteomes:UP000092714}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=373-A1 {ECO:0000313|EMBL:OBY10896.1,
RC ECO:0000313|Proteomes:UP000092714};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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 -!- 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:OBY10896.1}.
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DR EMBL; MAPZ01000019; OBY10896.1; -; Genomic_DNA.
DR RefSeq; WP_065254566.1; NZ_MAPZ01000019.1.
DR AlphaFoldDB; A0A1B8RQ52; -.
DR eggNOG; COG3437; Bacteria.
DR OrthoDB; 9804747at2; -.
DR Proteomes; UP000092714; Unassembled WGS sequence.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR037522; HD_GYP_dom.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR45228:SF1; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186; 1.
DR PANTHER; PTHR45228; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186-RELATED; 1.
DR Pfam; PF13487; HD_5; 1.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR PROSITE; PS51832; HD_GYP; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000092714}.
FT DOMAIN 5..119
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 146..343
FT /note="HD-GYP"
FT /evidence="ECO:0000259|PROSITE:PS51832"
FT MOD_RES 54
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 343 AA; 39635 MW; B592003FA60F1BC0 CRC64;
MKDFNLFYID DCKINHDVIA SFLKNIDINI EYFYDAISAL KCVNLKKPDI IIVDYIMPKM
NGLEFIKNVR SLDKKVPIIL ITAASDESIK LKALESGATE FLYLPFNKYE FIMRIKNLLE
LIKYQRRVEN KASILARGIK EATASIMERE KETLEVLVET AKKKDSDTGN HVVRVAKYSK
LLARVLGMSE EEQEEIYYAA QLHDLGKIGI SDQIINKRCQ LTLEEFEIMK THTIIGYDIL
KNRSSKYLKK GSIVALSHHE RYDGLVYPNG LKGNEIPIEG RIVAIADVFD ALLMKRSYKN
SWSIEEAIDY IKGKSGTQFD PYLVDRYIDN IEEIRRISYE FKD
//
