ID W7YEP9_9BACL Unreviewed; 888 AA.
AC W7YEP9;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Late competence protein ComEC {ECO:0000313|EMBL:GAF06987.1};
GN ORFNames=JCM16418_973 {ECO:0000313|EMBL:GAF06987.1};
OS Paenibacillus pini JCM 16418.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1236976 {ECO:0000313|EMBL:GAF06987.1, ECO:0000313|Proteomes:UP000019364};
RN [1] {ECO:0000313|EMBL:GAF06987.1, ECO:0000313|Proteomes:UP000019364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 16418 {ECO:0000313|EMBL:GAF06987.1,
RC ECO:0000313|Proteomes:UP000019364};
RA Yuki M., Oshima K., Suda W., Oshida Y., Kitamura K., Iida Y., Hattori M.,
RA Ohkuma M.;
RT "Draft Genome Sequence of Paenibacillus pini JCM 16418T, Isolated from the
RT Rhizosphere of Pine Tree.";
RL Genome Announc. 2:e00210-14(2014).
CC -!- FUNCTION: Counteracts the endogenous Pycsar antiviral defense system.
CC Phosphodiesterase that enables metal-dependent hydrolysis of host
CC cyclic nucleotide Pycsar defense signals such as cCMP and cUMP.
CC {ECO:0000256|ARBA:ARBA00034301}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic CMP + H2O = CMP + H(+); Xref=Rhea:RHEA:72675,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58003,
CC ChEBI:CHEBI:60377; Evidence={ECO:0000256|ARBA:ARBA00034221};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:72676;
CC Evidence={ECO:0000256|ARBA:ARBA00034221};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3',5'-cyclic UMP + H2O = H(+) + UMP; Xref=Rhea:RHEA:70575,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57865,
CC ChEBI:CHEBI:184387; Evidence={ECO:0000256|ARBA:ARBA00034227};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:70576;
CC Evidence={ECO:0000256|ARBA:ARBA00034227};
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:GAF06987.1}.
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DR EMBL; BAVZ01000002; GAF06987.1; -; Genomic_DNA.
DR AlphaFoldDB; W7YEP9; -.
DR STRING; 1236976.JCM16418_973; -.
DR eggNOG; COG0658; Bacteria.
DR eggNOG; COG2333; Bacteria.
DR Proteomes; UP000019364; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:InterPro.
DR CDD; cd07731; ComA-like_MBL-fold; 1.
DR Gene3D; 3.60.15.10; Ribonuclease Z/Hydroxyacylglutathione hydrolase-like; 1.
DR InterPro; IPR035681; ComA-like_MBL.
DR InterPro; IPR004477; ComEC_N.
DR InterPro; IPR004797; Competence_ComEC/Rec2.
DR InterPro; IPR025405; DUF4131.
DR InterPro; IPR001279; Metallo-B-lactamas.
DR InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR NCBIfam; TIGR00360; ComEC_N-term; 1.
DR NCBIfam; TIGR00361; ComEC_Rec2; 1.
DR PANTHER; PTHR30619; DNA INTERNALIZATION/COMPETENCE PROTEIN COMEC/REC2; 1.
DR PANTHER; PTHR30619:SF1; RECOMBINATION PROTEIN 2; 1.
DR Pfam; PF03772; Competence; 1.
DR Pfam; PF13567; DUF4131; 1.
DR Pfam; PF00753; Lactamase_B; 2.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019364};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 29..45
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 277..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..324
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 330..346
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 366..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..423
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 435..459
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 498..516
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 593..800
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 888 AA; 98750 MW; 4A7054F9F8AC4EE3 CRC64;
MKSRPLLMFT ICWILGSSCA YFASGTKLVM IWIGLSLLLA IPVILRRKTW GLVLMMWLAI
LLSGLYWEWK EIRNVSLLPE EFQQVILQQA DGLNVQAQGK VVSSVDVDGD RADFEVELEE
LSSSVVVGNG KGKEQGKVTH LSERVLVQVK LKVQSDQQQA GKWQRGDYVK LSGTMVKPAE
ARNFGGFDYG KYLRTQEVHW IYKVKGLSGV QCKPPASWSL GHILRWNDQV RDSLGAKLDL
LFHEPHAGYM KGLIIGMQDD LDPETFRQFS QLGLTHILAI SGMHVAVYVA VLLFILSLFR
VSRERALTIV MVLVPVYVLL SGLSPSVVRA GVMSIIALYA ARRGILKDGM NILAASALLM
LIWNPYYLLS VSFQLSFLVT AGLMVYVPLL QPLLRFMPQR LGAPLGVTLI AQLVSFPLTI
YYFNQFSLLS FAANFILVPV ITFLVLPLGT AALIIGSLWN MGGRGVAWIT ECLDDITFWL
VERMNDYPSF VTIWRSPSLV WIVMYYVLLY VLLYLARSWA VGRTPPVMQA DETVLLGDYK
ASGKKISFPN SEKQRYNLVM IPVLASLVIL MIFGYQPERR NGTGLVQFLD IGQGDSILIT
TPEGKNILVD GGGTVSFRKP EDAWKERRKP FEVGGKVLVP LLKQRGIHRL DAVILSHGDQ
DHAGGLQSVL DQIPVNAFFF NGTLAGTVSM DKLLSTALNR KIPLYAVHEG MVWSPDELTR
LDFIYPQTTQ EEQEMLFLEK NQNHASLVFI LSMGGSRFLF TGDMDKAAET ALLDSTFASP
SSKTTSASPK LSGSKVLPYL AAEGVDVIKV AHHGSKTSSS ASWLKAWQPK AAVISAGQNN
LYGHPHAEVV GRIKDQNATI YRTDQQGEIQ MLVKNGKIQI RYRILTKS
//
