ID B4VRC5_9CYAN Unreviewed; 789 AA.
AC B4VRC5;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Transglycosylase SLT domain protein {ECO:0000313|EMBL:EDX75441.1};
GN ORFNames=MC7420_1359 {ECO:0000313|EMBL:EDX75441.1};
OS Coleofasciculus chthonoplastes PCC 7420.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Coleofasciculus.
OX NCBI_TaxID=118168 {ECO:0000313|EMBL:EDX75441.1, ECO:0000313|Proteomes:UP000003835};
RN [1] {ECO:0000313|EMBL:EDX75441.1, ECO:0000313|Proteomes:UP000003835}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7420 {ECO:0000313|EMBL:EDX75441.1,
RC ECO:0000313|Proteomes:UP000003835};
RA Tandeau de Marsac N., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; DS989849; EDX75441.1; -; Genomic_DNA.
DR RefSeq; WP_006101151.1; NZ_DS989849.1.
DR AlphaFoldDB; B4VRC5; -.
DR STRING; 118168.MC7420_1359; -.
DR eggNOG; COG0457; Bacteria.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_013746_0_0_3; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000003835; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 3.
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; PF13174; TPR_6; 3.
DR SUPFAM; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000003835};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 628..740
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 789 AA; 89607 MW; 360DF6F7D36DBE95 CRC64;
MNKRREIFAP HSRSRRRQRR RQIALVAGVG LAGLIWGGTL IGGKYTRGLG QLTIRLPFVQ
HNSFNPEKQS DTAVLRLASL PANQRKAKLE AIAQGKNSID KSRARYLLAA DLIAQDKGKE
ALPWLEGLEL DYPVLGGYIA VKRAQAYEQI GEKTKALTEW QNLLQRYADQ PVAAYALHAL
FSKESQYQEE EINSLSANPS WQEKIQQMYE PPVDDPKYWE KAVANYPSHP LILELAGERL
QENPDQPELM LLLARYAFDT PEVTPDVTPI LDQLVGNYGR VVDSDNQPLI KPEDWQMIAV
GYWRDRKYGQ ASAAYAKAPE TSNNAYLVAR ALKFAQQYAD AKRAYKQMVS DFPDAEETPA
ALVELAQLQP DIEAVPYLDE VVERFPERAG EALLVKAETL ERLGSYQAAE EARKQLIDEY
GESDAAAAYR WQVARSHAES GNVEAAWEWA KPITTENPHR FLARQAGFWV GKWARELGHR
QDAQAAFEQV ITNHPQSYYA WRSAVQLGWD VGDFKTVRQL DPKLVLPKTR PLLPMGSAAL
KELYLLGQDE DAWILWKAEF QNRLEPTVAE QFTDGLVQLA IGDYLSGIST IASLENRETP
KEQAQYQDLR EKFTYWQALY PFPFSDKIAT YSQKRELNPL LVTALIRQES RFEPDIRSGA
GAVGLMQMMP STGEWAAENI DMENYSLENP DDNIKLGTWF LREVHQSYND NSLLAIASYN
AGQGNLSKWL QQDSAGDPDE FVESIPFDET RDYVKQVFGN YWNYLRLYDP KVAQQVAQHS
QSQSTAMRR
//
