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Database: UniProt
Entry: A0A0R2I787_CARDV
LinkDB: A0A0R2I787_CARDV
Original site: A0A0R2I787_CARDV 
ID   A0A0R2I787_CARDV        Unreviewed;       502 AA.
AC   A0A0R2I787;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=SPOR domain-containing protein {ECO:0000259|PROSITE:PS51724};
GN   ORFNames=IV74_GL000127 {ECO:0000313|EMBL:KRN57149.1};
OS   Carnobacterium divergens DSM 20623.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC   Carnobacterium.
OX   NCBI_TaxID=1449336 {ECO:0000313|EMBL:KRN57149.1, ECO:0000313|Proteomes:UP000051658};
RN   [1] {ECO:0000313|EMBL:KRN57149.1, ECO:0000313|Proteomes:UP000051658}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 20623 {ECO:0000313|EMBL:KRN57149.1,
RC   ECO:0000313|Proteomes:UP000051658};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 73 family.
CC       {ECO:0000256|ARBA:ARBA00010266}.
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:KRN57149.1}.
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DR   EMBL; JQBS01000007; KRN57149.1; -; Genomic_DNA.
DR   RefSeq; WP_051915679.1; NZ_JQLO01000001.1.
DR   AlphaFoldDB; A0A0R2I787; -.
DR   PATRIC; fig|1449336.4.peg.128; -.
DR   eggNOG; COG1705; Bacteria.
DR   Proteomes; UP000051658; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR   GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR   Gene3D; 1.10.530.10; -; 1.
DR   InterPro; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR   InterPro; IPR007730; SPOR-like_dom.
DR   PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR   Pfam; PF01832; Glucosaminidase; 1.
DR   PRINTS; PR01002; FLGFLGJ.
DR   SMART; SM00047; LYZ2; 1.
DR   PROSITE; PS51724; SPOR; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051658};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          303..382
FT                   /note="SPOR"
FT                   /evidence="ECO:0000259|PROSITE:PS51724"
FT   REGION          24..79
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..63
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   502 AA;  56671 MW;  6B7B674613088204 CRC64;
     MYSSLFLLCS TTLPLNVLAE KVQSNESSLK SVDIPDSTEP EATNVTTNDH LDNSASSSSN
     EETENKENTT ENEIPPNDID ISKTYSQEAA WSAAMNKQPE IFSRSFMSSE SFIDSIAPHA
     VKVATERGLY PSVMMAQAIL ESGWGKSGLA SAPNYNLFGI KGSYKGQSVM FPTWEFINGQ
     WVTVQAAFRK YPSYTQSFED NGDLLRNGLT GDPNFYSGTW VSNTSSYRDA TQWLQGRYAT
     DPTYASKLNS TIEANNLTQY DTIQKNYRIS IEDLNFVSPT YAKQAQEQLT SVFPIWSTVV
     PSNQMKNYAY IQTGDFLNKV DAEQVNKNFM TSTGFWASVE KSDKSRPYYR VETGGFLGKQ
     TADMVLSKFI KDTGWWAEVV PTGEQNKYKI ITGDFLDPLD QDSVVRYFAS EKWWSTGFVS
     QKTPEPYYKI VTGNYLNHPD AVKSSKDFFA ANNVWAQSLD STLQFQLYKI NTGGFGTYEN
     TLHWKTMMES KFNWNMTIEE DL
//
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