ID K9Z178_CYAAP Unreviewed; 727 AA.
AC K9Z178;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Lytic transglycosylase catalytic {ECO:0000313|EMBL:AFZ52919.1};
GN OrderedLocusNames=Cyan10605_0786 {ECO:0000313|EMBL:AFZ52919.1};
OS Cyanobacterium aponinum (strain PCC 10605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ52919.1, ECO:0000313|Proteomes:UP000010480};
RN [1] {ECO:0000313|Proteomes:UP000010480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP003947; AFZ52919.1; -; Genomic_DNA.
DR RefSeq; WP_015218650.1; NC_019776.1.
DR AlphaFoldDB; K9Z178; -.
DR STRING; 755178.Cyan10605_0786; -.
DR KEGG; can:Cyan10605_0786; -.
DR PATRIC; fig|755178.3.peg.827; -.
DR eggNOG; COG0741; Bacteria.
DR eggNOG; COG1729; Bacteria.
DR eggNOG; COG4105; Bacteria.
DR HOGENOM; CLU_013746_0_0_3; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000010480; Chromosome.
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 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; 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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000010480};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 577..689
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 727 AA; 83589 MW; AF4FCBE1A46D4DEB CRC64;
MKTDKSKKNQ VIIQIVVILA VCVAGATFFT PKLLEILNSV LISPFEKKPE YRLDAPSEVL
PLANLTPSER KASLEVIANK DTSSLDVNRA KYLLAVDALR NDFDGAKALQ YLENLDRTYP
ILAPYVLLLQ GRAYELNNNT EKAQKIWQDV INKYPDELVS AQAYYKLGNY DPKFFQEAIN
RFPQHPRTHD IAIKLLEENP QQKELLLLLA EYDIVPENKA RVDRLVKEYS QELEPQQWDI
VGNYYWETGN YNLVSSAYEK GTSTPQNLYR IARSYQVSDK EKEAKTAYFK LVETYPDAPE
TGLAWRRLAT ISGGEEALSF LNRVDEKYPD EVVIALREKA TLLTQLGRYQ EATNVRDTIL
QKYPQSEEAA DYRWQIAKDF ADSGDYVSAW QWAQQISVNN PDSGVAPKAG FWIGKWAEKL
GQNQEATKAY EYVLQNHPHS YYAWRSAVRL GKDVGDFNNL RSLPLQVEIP QQRPIPPAGS
NQFKELFLLG EDQDAIDLFT AEIGKKSSST DTLPVVTVSE QFVQGLLKQN QGKYLESINL
IWNLKNRDNP EDIGEWQILR RSPEYWYALF PFPYEELIVK WSKKRNLNPF LVVSLMRQES
RFEKDIKSPV GATGLMQIMP ETGAWIAPQI NIKEYSLTDP EDNIKMGTWY LNYTHDTYND
NSMLAIASYN AGPGNVSNWI SRYSLADIDE FVENIPFPET KNYVETVFGN YWNYVELYDP
KIEEKLN
//