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Database: UniProt
Entry: A0A0P4UNT9_9CYAN
LinkDB: A0A0P4UNT9_9CYAN
Original site: A0A0P4UNT9_9CYAN 
ID   A0A0P4UNT9_9CYAN        Unreviewed;       726 AA.
AC   A0A0P4UNT9;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Soluble lytic murein transglycosylase {ECO:0000313|EMBL:GAP95948.1};
GN   ORFNames=NIES2104_24770 {ECO:0000313|EMBL:GAP95948.1};
OS   Leptolyngbya sp. NIES-2104.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae;
OC   Leptolyngbya group; Leptolyngbya.
OX   NCBI_TaxID=1552121 {ECO:0000313|EMBL:GAP95948.1, ECO:0000313|Proteomes:UP000052243};
RN   [1] {ECO:0000313|EMBL:GAP95948.1, ECO:0000313|Proteomes:UP000052243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NIES-2104 {ECO:0000313|EMBL:GAP95948.1,
RC   ECO:0000313|Proteomes:UP000052243};
RX   PubMed=26494835; DOI=10.1093/dnares/dsv022;
RA   Shimura Y., Hirose Y., Misawa N., Osana Y., Katoh H., Yamaguchi H.,
RA   Kawachi M.;
RT   "Comparison of the terrestrial cyanobacterium Leptolyngbya sp. NIES-2104
RT   and the freshwater Leptolyngbya boryana PCC 6306 genomes.";
RL   DNA Res. 22:403-412(2015).
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
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:GAP95948.1}.
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DR   EMBL; BBWW01000001; GAP95948.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P4UNT9; -.
DR   STRING; 1552121.NIES2104_24770; -.
DR   InParanoid; A0A0P4UNT9; -.
DR   Proteomes; UP000052243; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   CDD; cd13401; Slt70-like; 1.
DR   Gene3D; 1.10.530.10; -; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 2.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   PANTHER; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR   PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR   Pfam; PF01464; SLT; 1.
DR   Pfam; PF13432; TPR_16; 1.
DR   Pfam; PF13174; TPR_6; 1.
DR   SUPFAM; SSF48435; Bacterial muramidases; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Signal {ECO:0000256|ARBA:ARBA00022729}.
FT   DOMAIN          566..680
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   726 AA;  80792 MW;  A2C97065B7F7D7F7 CRC64;
     MILASGAGAI GLIAGALLPI EKLRQVSEMP SGVVSSIQSL NSPQPSGIGT PSTVISPLVT
     KSANERGAAL KQVTQSASST LERDRARYLL AVDLISQNQG EKALEQLKDL EKSYPVLAAQ
     IGVKRAQAYE VSGKQKEAAQ TLQEVVKQLP KEPATAEALF TLGKKDSKFW DQALQQFPSH
     PRSIEIARTR LKQNPKQFPL LMLVARYGTD SEGYTELLDR IVSQFSNQLK PEDWEAIAFG
     YWENQVYDKG AIAYSRAPQT SLTAYRSARG LHLSGKPGAT ERYRQMVQQF PQSSEAGLAL
     TRLADLAETP QMAIAYLDQV IQNFPDRAPA ALVEKSKMLD KMNSGKTAAQ MRQLVLTQYA
     NSDAAAEMRW EYAQKSAKAG NIKLARQWAE PILTNNSTSE IAAEAGFWSG KWAQTIGNND
     QAAKLFQKVL SDHPESYFAW RSASILGWNV GDFNSVRSMN PQVQKPLSRP ELPAGSPALK
     ELYQLGQERA AWSHWQIEFQ NRVKPSIAEQ FTDGVMRLGV GDNLDAIYMV GSLRDRDTPE
     DKAQYQQLRK NIGYWQALYP FPFVETIENW SQQRQINPML VTALIRQESR FEPNIRSSVG
     AVGLMQVMPE TGQYIANNIK VKEFKLADPE TNIKFGTWYL DYTHAQYSNN SLLAVASYNA
     GPGAVSGWLS KAKTQDPDEF VESIPYSETR GYVKSVLGNY WNYLRLYNPE ISQRVSQVAA
     DHPKGN
//
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