ID A0A0S8I010_9CHLR Unreviewed; 803 AA.
AC A0A0S8I010;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Transglycosylase SLT domain-containing protein {ECO:0000259|Pfam:PF01464};
GN ORFNames=AMJ88_15100 {ECO:0000313|EMBL:KPK90899.1};
OS Anaerolineae bacterium SM23_ 63.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703387 {ECO:0000313|EMBL:KPK90899.1, ECO:0000313|Proteomes:UP000051685};
RN [1] {ECO:0000313|EMBL:KPK90899.1, ECO:0000313|Proteomes:UP000051685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_ 63 {ECO:0000313|EMBL:KPK90899.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(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:KPK90899.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LJUS01000065; KPK90899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8I010; -.
DR Proteomes; UP000051685; Unassembled WGS sequence.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
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; PF13432; TPR_16; 3.
DR Pfam; PF13174; TPR_6; 2.
DR SMART; SM00028; TPR; 9.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR SUPFAM; SSF48452; TPR-like; 3.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS50005; TPR; 2.
PE 3: Inferred from homology;
KW TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT REPEAT 202..235
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT REPEAT 473..506
FT /note="TPR"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT DOMAIN 670..766
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 803 AA; 90412 MW; 8BDA502F9C7C0EBB CRC64;
MRWPRLRGIF ILLCLIFSTL ACNLPELLGV GPTPTPSMTP TATITPTATP TPTPLPSARL
DSARWALFKG DWEVALSEYQ ISLAQAVDPD EQANAQLGIG LAMLNSNRYQ EAVDALTLYL
ESYPFHDLLG QGYFHRAQAQ AAAGQFEAAA NDYGQYLLLR TGLIDSFVHE RRGDALREAG
NPAEAIVAFQ NALVSPRLGD DLELEIKIGR AYLEMGDYNA ALAKYNDVFE RATSDYTKAQ
MDFARGRVHA ALGQFDQAYG FYLHAVENYP LSYDTYLGLV ELVEAGVAVN ELDRGLVDYY
AGQHGVAVAA FNRYLAAAPM DHDGTVHYYK GLSQRALGAY VDAIDEWDIL IDTHTTDRYW
DEAWEEKAFT QWAYLDQYDA AAQTLLNFVA TVPDHVRAAE YLYDAARIKE RSDQLDEAAS
IWQRLGVEYP NSEWTYRGLF LAGIARYRLS DFLGSEDVFL KCLEIAGESS DLAAAYLWLG
KTYMARGDAV SAQTAWQRAV ESHPHGYYGL RAGDLLLGRE PFQPIGVFNF HYDEETERFE
AEEWLREHFP ITGPDPLSAL DPVLANDARI VRGDEYWQLG LFDQAKAEFE SLRLEKENDA
EATYRLMHHF LDLGFYRPAI YAAWRILDLA DIAEMGINAA PIYFSRIRFG PYFGDLIMPE
ALRHDFDGLF VLSVIRQESL FEGFAISYAD ARGLMQIIPS TGQSIVDQLG WPPGYTDLDL
YRPVVSVRLG VQYLSTQRET FDGDLYAALS AYNAGPGNAI IWKAIAPEDP DLFLEVIRLQ
QPQDYIRYIY WAFTNYQALY SEP
//
