ID A0A3B0C0N2_9BACL Unreviewed; 858 AA.
AC A0A3B0C0N2;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=DNA internalization-related competence protein ComEC/Rec2 {ECO:0000313|EMBL:RKN79032.1};
GN ORFNames=D7M11_21930 {ECO:0000313|EMBL:RKN79032.1};
OS Paenibacillus ginsengarvi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=400777 {ECO:0000313|EMBL:RKN79032.1, ECO:0000313|Proteomes:UP000282311};
RN [1] {ECO:0000313|EMBL:RKN79032.1, ECO:0000313|Proteomes:UP000282311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13059 {ECO:0000313|EMBL:RKN79032.1,
RC ECO:0000313|Proteomes:UP000282311};
RX PubMed=17684262; DOI=10.1099/ijs.0.64906-0;
RA Yoon M.H., Ten L.N., Im W.T.;
RT "Paenibacillus ginsengarvi sp. nov., isolated from soil from ginseng
RT cultivation.";
RL Int. J. Syst. Evol. Microbiol. 57:1810-1814(2007).
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:RKN79032.1}.
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DR EMBL; RBAH01000017; RKN79032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3B0C0N2; -.
DR OrthoDB; 9761531at2; -.
DR Proteomes; UP000282311; 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; 1.
DR SMART; SM00849; Lactamase_B; 1.
DR SUPFAM; SSF56281; Metallo-hydrolase/oxidoreductase; 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:UP000282311};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 40..58
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 63..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 303..325
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..348
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 354..371
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..417
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..448
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..472
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 525..545
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 552..569
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 587..812
FT /note="Metallo-beta-lactamase"
FT /evidence="ECO:0000259|SMART:SM00849"
SQ SEQUENCE 858 AA; 94525 MW; D3B78442A5EE4185 CRC64;
METKVYDVKH PIKRPLATAA VLWTAGTALG GELPQGLLSW KAFMLSVALG VMLALFAIPG
RRIIGLLLVV MAAAAYYQIY DAKNVPTIPM PSVVETESGD PAAGSVGREV RLTGEIASRV
EVDGDKVSFA LRSQAVRLDE EEPLQASDTV QVSVRLLQQE EQVRARTMGR GDPVTVSGVL
KRPDLPRNFG GFDYRLYLYR NHIHWQLSAK GLDSVLTEAE ADEEEVEGSL LAERRNRFAF
VPEPVRIMRW NDDLRSRLGA VFDSLFPMGG PDSGYLKSLV IGLTDDMDPE LYRHFSQLGL
THILAISGLH VGVFVAGCMW LLRLFGLTRE RILTVTLLLV PFYVAIAGGS PSAVRAGIMA
MIGLYAARRL LWKDAPNVIG LAAILMLLWE PYFLYNVSFQ LSFLVTTGLI VGVQRFSRLL
PIRNKSVSSL LSITIVAQVI SFPVTVYYFN GISLLSMLAN LVMVPFISFV VLPLGTFALL
AGLVSVHAGA PFGWIVEKVN RLTFWLIDYA ATHDPSQFIW PKPSIAWIVA YYGLLAAVYA
GAIRWKEEQK PLLAYAAVPL MMALLWFGYN PDMLDRDGKV SFIDVGQGDA ILIRTPQQRH
VLIDGGGTLS FRKPGEEWKE RSDPYEVGKK LLVPLLKQRG VHRIDQLVIS HQDQDHIGGL
QAVVEQIPVT TIVMNGTWKG NASSRKLFET AMRKGTAIVS IAPGGLTPVD RYTKLTVLSS
GGGKPTRVAE EQNNESVVLL LQMRDARFLF TGDMRAEDEK ELLAAWQTAA AEEEVPEPVD
VMKIAHHGSK TSSSGEWLSY WKPERAVISV GLNNSYGHPN AGVLERIAEA GSVIYRTDRS
GEIVFTVTRT GLTVDSKL
//
