ID A0A0F0CBZ5_9CLOT Unreviewed; 1261 AA.
AC A0A0F0CBZ5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Stage 0 sporulation protein A homolog {ECO:0000256|ARBA:ARBA00018672};
GN Name=rpfG_4 {ECO:0000313|EMBL:KJJ69733.1};
GN ORFNames=CLFS41_37860 {ECO:0000313|EMBL:KJJ69733.1};
OS Clostridium sp. FS41.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1609975 {ECO:0000313|EMBL:KJJ69733.1, ECO:0000313|Proteomes:UP000033604};
RN [1] {ECO:0000313|EMBL:KJJ69733.1, ECO:0000313|Proteomes:UP000033604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FS41 {ECO:0000313|EMBL:KJJ69733.1,
RC ECO:0000313|Proteomes:UP000033604};
RA Poehlein A., Daniel R.;
RT "Genome sequencing of Clostridium sp. FS41.";
RL Submitted (FEB-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 -!- 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:KJJ69733.1}.
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DR EMBL; JYHN01000064; KJJ69733.1; -; Genomic_DNA.
DR RefSeq; WP_045093146.1; NZ_JYHN01000064.1.
DR AlphaFoldDB; A0A0F0CBZ5; -.
DR PATRIC; fig|1609975.3.peg.4054; -.
DR Proteomes; UP000033604; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR CDD; cd01949; GGDEF; 1.
DR CDD; cd00077; HDc; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.30.70.270; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR000160; GGDEF_dom.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR037522; HD_GYP_dom.
DR InterPro; IPR029787; Nucleotide_cyclase.
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 InterPro; IPR043128; Rev_trsase/Diguanyl_cyclase.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00254; GGDEF; 1.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45228:SF1; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186; 1.
DR PANTHER; PTHR45228; CYCLIC DI-GMP PHOSPHODIESTERASE TM_0186-RELATED; 1.
DR Pfam; PF00990; GGDEF; 1.
DR Pfam; PF13487; HD_5; 1.
DR Pfam; PF08447; PAS_3; 2.
DR Pfam; PF00072; Response_reg; 1.
DR SMART; SM00267; GGDEF; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 3.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50887; GGDEF; 1.
DR PROSITE; PS51832; HD_GYP; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW Hydrolase {ECO:0000313|EMBL:KJJ69733.1};
KW Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW Reference proteome {ECO:0000313|Proteomes:UP000033604}.
FT DOMAIN 6..123
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 143..351
FT /note="HD-GYP"
FT /evidence="ECO:0000259|PROSITE:PS51832"
FT DOMAIN 556..595
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 598..649
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 726..778
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 809..942
FT /note="GGDEF"
FT /evidence="ECO:0000259|PROSITE:PS50887"
FT MOD_RES 56
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1261 AA; 144296 MW; 07D13149E3FAABA7 CRC64;
MRQRDTILIV DDMEINRVIL SGLFQDEYHL LEAENGEQAL LLLKQYHSNI AIMLLDVVMP
VMDGYQVMKE MGAGGFLDEV PVVVITADNS LEGELRSFDL GASDIIVKPF EPHVVKRRVH
NIIELYLHKH NLEDMVDHQA RKLKESNDIL VDALSSVIEY RSLESGQHIK RIRLLTRVLL
EEVSKNCPEY GLDQQKIEVI ASASALHDIG KIAIEDRILN KPGRLTPEEF EIMKTHTIKG
CQILDSLGRM SDKEYLQYAY NICHYHHERW DGKGYPEGLC KDAIPICAQA VSVVDAYDAL
TSDRVYKNAI PYQQAANMIL NGECGAFSPK MLECFKTVQP ALAGLCRQYA DGNVPREHSL
SQEASLMPVA EGSVSALQLE QMKYLAMLRY ENTMVVEVDF STGSYHMVYA PNLRIKRSFQ
GERLEDAVGR YIAEMVDPQD QEYMREAWAM GMPGFFQQGM LKKSWKHRVR DGQGWCWFDL
TILRIDIEHP RQRKALLLWK ALEAEAEHIS AGRTGGQQET GEELQDDVQI LHSILKGISR
YRNDQWFTIL EIDDGFMGYG RDEINGRFHG HYLDMIHPDD RTRVKKELSD QLNHGNEFEL
EYRVQDADGV SNWVLGKGCL ITDQDGQECL YSVIIDINQT KRAQEELRLG LERYKIIMEQ
TNDIFFEWDI ETDTVNYSPN WKGKFGYDPI SARASERIPK ISHLHPEDMA PFGAFIQQIR
SGRRYGELEF KVSDSRGRYQ WCKLRATTQF DDQGKPCKAI GIVIDINEEK MAAQELKARA
ERDTLTRLYN KASARQRIEY LLANREKPEG AALFIIDIDN FKMVNDQYGH MFGDAVLTKI
ASQLSRLFRS SDIVSRIGGD EFMALLQGVL GDEQVKMVAG RILECFDRVL EELPRECSIT
SSIGIAVCPR DGDDFQTLFQ RADVALYHAK ACGKNQYQIY DQSMESRAYG QNAGRQTAAN
TTIESEGTEL VLSDLLPRAF NILSKAEQLD RAVESVLELL GERLQVSRAY VFENSEDNLF
YSNTFEWCAE GIEPQKDKMQ NMAYSEFDSD YRDYFNERGI LYCDDIGKFP RDIRELMESQ
GIQSMLQCAI KDNGVFKGWV GFDDCTSKCL WTINQIEVLS FISELLSLFL LKQRAQDNVM
ELAGDLRAVL DHQNSWIYVV DIGTRELLYI NEKTQRIAPE AKLGMSCHKA FFGRKEPCAR
CPMEDIRHKI NCTMEVYNPL LKVWSLADAS VIRWGKKDAC LLACHDITRY KTGKDGPDQE
K
//
