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Database: UniProt
Entry: A0A1H1ZKZ0_9BACL
LinkDB: A0A1H1ZKZ0_9BACL
Original site: A0A1H1ZKZ0_9BACL 
ID   A0A1H1ZKZ0_9BACL        Unreviewed;       901 AA.
AC   A0A1H1ZKZ0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Competence protein ComEC {ECO:0000313|EMBL:SDT34289.1};
GN   ORFNames=SAMN05444162_3898 {ECO:0000313|EMBL:SDT34289.1};
OS   Paenibacillaceae bacterium GAS479.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae.
OX   NCBI_TaxID=1882832 {ECO:0000313|EMBL:SDT34289.1, ECO:0000313|Proteomes:UP000198637};
RN   [1] {ECO:0000313|EMBL:SDT34289.1, ECO:0000313|Proteomes:UP000198637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS479 {ECO:0000313|EMBL:SDT34289.1,
RC   ECO:0000313|Proteomes:UP000198637};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; LT629764; SDT34289.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1ZKZ0; -.
DR   STRING; 1882832.SAMN05444162_3898; -.
DR   OrthoDB; 9761531at2; -.
DR   Proteomes; UP000198637; Chromosome i.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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; IPR025405; DUF4131.
DR   InterPro; IPR001279; Metallo-B-lactamas.
DR   InterPro; IPR036866; RibonucZ/Hydroxyglut_hydro.
DR   NCBIfam; TIGR00360; ComEC_N-term; 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   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:UP000198637};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        54..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        323..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        366..385
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        391..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        423..443
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        599..618
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          49..225
FT                   /note="DUF4131"
FT                   /evidence="ECO:0000259|Pfam:PF13567"
FT   DOMAIN          270..537
FT                   /note="ComEC/Rec2-related protein"
FT                   /evidence="ECO:0000259|Pfam:PF03772"
FT   DOMAIN          628..852
FT                   /note="Metallo-beta-lactamase"
FT                   /evidence="ECO:0000259|Pfam:PF00753"
SQ   SEQUENCE   901 AA;  98221 MW;  43BC55D04BD0609B CRC64;
     MDLAGDEGCQ IDPREGGMRL EARGWLDGRP LVWAAVCFVA GSSAAAYWSP GGMLAAGLGL
     GLLLAALALA GQARYGLAAA CLAAYALAAG ERLWADARSQ TALSALYAAA EAQLEPPELR
     VEAAGTVVSP VEFDGDLVQL RLEAHSLRAG DAQQAKPLRE TLLVRVKLLH EQELAAAKAW
     RRGNSVRLRG TLELPAPPAN RGGFDYRRYL RSQGITWLLQ VQGAGAVQAA PGKSHSAAAL
     LGRMDAARAQ LGSALTRIYP ADQAGYMQAL VLGNQDETDP ELYRRFARLG LTHIMAVSGM
     HVAVMLGLLG FSLRQLRLTK ERILLLLMFA VPPYVLFTGA SPSILRAGLM ALLGLAAARA
     GKLKDGLHLL AASAVLLLLW NPRLIESVSF QLSYIVTAGL ILGVPAVNRL LSRPRSRLRF
     VQDAVVVTFV AQAISFPVTI YYFNQIHLLS LPANLLLVPF ISFLIMPAGA AVMLVEPIWP
     GAAQLLANWS TEANMWTFRL IEWMGEWSDG STIWATPSLW WIVSYYAVLF GLLQSLGRWR
     SCKQAAAEET CFSDNEDTQP LLPVKDTSRY SPSTAPAMSV QTRIRNVASS LRSPLTRSVL
     TGSILLLLLL HAFHSGWYDR AAYVQFLNVG QGDAILIRTP SGQTILIDGG GTMQFRREAW
     RQRRDPYEIG RKMLVPLLMK RGVSEIDLLV VTHLDQDHIG GLEAVLDGIP VKRLLWNGSL
     KEAGETPPLL QRAINKGIPL YGAEAGMSWQ PDVSTRLDVL WPTKHNDMQP IEEQNEQSVV
     LLLTLFNRSF LLAGDLGSVS ESAVMETAKS LALPARNTPI DVLKAGHHGS KNSTSAAWLS
     YWKPSVSVLS AGIDNRYGHP SEDVLMRLKQ FSSRAVRTDL NGEIEFRVTP QGMDMRLLRG
     N
//
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