ID A0A0B8ZZ63_BRELN Unreviewed; 731 AA.
AC A0A0B8ZZ63;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=LPXTG-motif cell wall anchor domain protein {ECO:0000313|EMBL:KHS51765.1};
DE EC=3.1.4.16 {ECO:0000313|EMBL:KHS51765.1};
GN ORFNames=AE0388_2315 {ECO:0000313|EMBL:KHS51765.1};
OS Brevibacterium linens.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Brevibacteriaceae;
OC Brevibacterium.
OX NCBI_TaxID=1703 {ECO:0000313|EMBL:KHS51765.1, ECO:0000313|Proteomes:UP000031488};
RN [1] {ECO:0000313|EMBL:KHS51765.1, ECO:0000313|Proteomes:UP000031488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AE038-8 {ECO:0000313|EMBL:KHS51765.1,
RC ECO:0000313|Proteomes:UP000031488};
RA Maizel D., Utturkar S.M., Brown S.D., Ferrero M., Rosen B.P.;
RT "Draft Genome Sequence of Brevibacterium linens AE038-8.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the 5'-nucleotidase family.
CC {ECO:0000256|RuleBase:RU362119}.
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:KHS51765.1}.
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DR EMBL; JTJZ01000020; KHS51765.1; -; Genomic_DNA.
DR RefSeq; WP_039210525.1; NZ_JTJZ01000020.1.
DR AlphaFoldDB; A0A0B8ZZ63; -.
DR STRING; 1703.BLSMQ_1634; -.
DR PATRIC; fig|1703.6.peg.2214; -.
DR OrthoDB; 1016457at2; -.
DR Proteomes; UP000031488; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008663; F:2',3'-cyclic-nucleotide 2'-phosphodiesterase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008252; F:nucleotidase activity; IEA:UniProt.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0009166; P:nucleotide catabolic process; IEA:InterPro.
DR Gene3D; 3.60.21.10; -; 1.
DR Gene3D; 3.90.780.10; 5'-Nucleotidase, C-terminal domain; 1.
DR InterPro; IPR008334; 5'-Nucleotdase_C.
DR InterPro; IPR036907; 5'-Nucleotdase_C_sf.
DR InterPro; IPR006146; 5'-Nucleotdase_CS.
DR InterPro; IPR006179; 5_nucleotidase/apyrase.
DR InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR InterPro; IPR019931; LPXTG_anchor.
DR InterPro; IPR029052; Metallo-depent_PP-like.
DR NCBIfam; TIGR01167; LPXTG_anchor; 1.
DR PANTHER; PTHR11575:SF6; 2',3'-CYCLIC-NUCLEOTIDE 2'-PHOSPHODIESTERASE_3'-NUCLEOTIDASE; 1.
DR PANTHER; PTHR11575; 5'-NUCLEOTIDASE-RELATED; 1.
DR Pfam; PF02872; 5_nucleotid_C; 1.
DR Pfam; PF00746; Gram_pos_anchor; 1.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR01607; APYRASEFAMLY.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00785; 5_NUCLEOTIDASE_1; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|RuleBase:RU362119, ECO:0000313|EMBL:KHS51765.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362119};
KW Peptidoglycan-anchor {ECO:0000256|ARBA:ARBA00023088};
KW Reference proteome {ECO:0000313|Proteomes:UP000031488};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Signal {ECO:0000256|RuleBase:RU362119};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT CHAIN 24..731
FT /evidence="ECO:0000256|RuleBase:RU362119"
FT /id="PRO_5002127203"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 46..287
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
FT DOMAIN 381..555
FT /note="5'-Nucleotidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02872"
FT DOMAIN 695..730
FT /note="Gram-positive cocci surface proteins LPxTG"
FT /evidence="ECO:0000259|Pfam:PF00746"
FT REGION 596..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..633
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 653..675
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 731 AA; 77556 MW; 0AA15801FE0CDE10 CRC64;
MRLRTLTSSS LALALIVTGP AAASATGLGS ADAPADSQAA KTAELTLLAT TDVHGNVLNW
DYFANKPYPA GEELGMSRAS TLIKGVREDK GAESVLLVDN GDTIQGNPLA YYFAKQEPIT
TSGQTHPLAK TYNHLGYDAQ VVGNHEFNYG LDLLGTYRDQ VDFPLLGANV IDDADGQTHL
DPYELVDKQV DGETITVGVL GMTTPGSRIW DKNNLSGKVH FDDPVETAEK YVPEMKQKGA
DVIVVLSHSG KDPKGQTWDP DQLQENVSTS VAKVPGIDVL VAGHTHQNEP SQVVNRDDGS
QVLITQPNYW ARSVSEVGLP INLDTHHVDW GENEPHADAL ATQGEIAEDQ EIKDLVDEQH
RTTIDYVNTK IGSVTETLWA KTSYYEDTAI LDFISHVQTE KVEEGLKGTD YEGLPVISQA
SPFSRTAEFP AGDITIRDVA GLYVYDNTLA GVEINGAQLR DYLEYSARYF KQTEEGAEFD
PVDGTNAIDE VLESPIPDYN YDALAGIDYD INVSKPTGER IENLKQADGS AIGDDDRFIL
AINNYRQSGG GGYPVDGLKE VYNEQVEVRQ ALIDWAKAKQ VVDPADFFDE NWQVVTSSRA
PGGDDDSNDD EDADSSGEAT AEADSNGSDG GGSDAGGSSD AAGAGSDGSS DGADNAGAAT
SEEDDSTNGA SDGGASDSNA DEGDADDSTV GAGGGADLPR TGLEVATSIG IAAAIIALGT
ALVVFSRRRR G
//
