ID A0A0C1R2V4_9CLOT Unreviewed; 691 AA.
AC A0A0C1R2V4;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=LPXTG cell wall anchor domain protein {ECO:0000313|EMBL:KIE47857.1};
GN ORFNames=U732_3596 {ECO:0000313|EMBL:KIE47857.1};
OS Clostridium argentinense CDC 2741.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1418104 {ECO:0000313|EMBL:KIE47857.1, ECO:0000313|Proteomes:UP000031366};
RN [1] {ECO:0000313|EMBL:KIE47857.1, ECO:0000313|Proteomes:UP000031366}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 2741 {ECO:0000313|EMBL:KIE47857.1,
RC ECO:0000313|Proteomes:UP000031366};
RX PubMed=25489752; DOI=10.1016/j.meegid.2014.12.002;
RA Smith T.J., Hill K.K., Xie G., Foley B.T., Williamson C.H., Foster J.T.,
RA Johnson S.L., Chertkov O., Teshima H., Gibbons H.S., Johnsky L.A.,
RA Karavis M.A., Smith L.A.;
RT "Genomic sequences of six botulinum neurotoxin-producing strains
RT representing three clostridial species illustrate the mobility and
RT diversity of botulinum neurotoxin genes.";
RL Infect. Genet. Evol. 30:102-113(2014).
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:KIE47857.1}.
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DR EMBL; AYSO01000013; KIE47857.1; -; Genomic_DNA.
DR RefSeq; WP_052267970.1; NZ_AYSO01000013.1.
DR AlphaFoldDB; A0A0C1R2V4; -.
DR STRING; 29341.RSJ17_17975; -.
DR OrthoDB; 9800780at2; -.
DR Proteomes; UP000031366; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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:0005975; P:carbohydrate metabolic process; 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; IPR019079; Capsule_synth_CapA.
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 SMART; SM00854; PGA_cap; 1.
DR SUPFAM; SSF55816; 5'-nucleotidase (syn. UDP-sugar hydrolase), C-terminal domain; 1.
DR SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
DR PROSITE; PS00786; 5_NUCLEOTIDASE_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Hydrolase {ECO:0000256|RuleBase:RU362119};
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:UP000031366};
KW Secreted {ECO:0000256|ARBA:ARBA00022512};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 664..681
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 87..275
FT /note="Capsule synthesis protein CapA"
FT /evidence="ECO:0000259|SMART:SM00854"
FT REGION 619..648
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 628..648
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 691 AA; 76927 MW; 6D28F43745DF71E0 CRC64;
MLKLFKMKKT ISLLVVFTMV FTLFSFHSTK EVFANEETKE IQIIGTSDLH GRFAPYEYAM
NEANTKGSLS QISSLIKELK EKNPNTMVVD AGDTVQDNSS QLFLKDDIHP MVLAMNEIGY
DTWTLGNHEF NYGVPALEKM MSQFTNTSIL CGNVYKPNGE PLGKAYEIVD INGVKVANIG
MVSPHITKWD GPNLEGYKVT NPVEETKKAV KEIQDNKKAD IIIATVHMGK DTEYGLGDSA
SEIAEACPEI AAIICGHAHS TIKGEVVNGV IITEPGKYGE FVSKIDIKLT KNSDGKYVIK
NRSTDIKSDL IEVKTYKEDE ALKSKLAPQH EKALADANII IGELKGGDLA PANEIKGITE
AQLRDTPLLD LILEVQMHYG KKNVPNGAHH VSAAAIFDSK ANAKEGKIKK ADTSKIYKYD
NTLMTLKING NQLKKYMEWS AKYYNTFKEG DLTVSFNEKI RMYNYDMFGG IKYEINISKP
EGSRIENLTY NDGTAVKDGD IIYLTVNNYR ANTTLLNSDS GIFKGENVEV VYDSANEQLS
AVRDFIREYI VKEKNGVITP TLDNNWKLTG YNFDKSKRDA AVKLINEGKV DIPTSEDGRT
PNVRSVTWED IKHLVPELPD IKDNEVTNPE GKPSSNDNNN NNSNNNFEEE KLPQTGLEFG
SEDFISLGSL VSLLGISMFL FNKKKKNEDA A
//
