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Database: UniProt
Entry: B9M5H6_GEODF
LinkDB: B9M5H6_GEODF
Original site: B9M5H6_GEODF 
ID   B9M5H6_GEODF            Unreviewed;       717 AA.
AC   B9M5H6;
DT   24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   24-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   SubName: Full=Lytic transglycosylase domain protein {ECO:0000313|EMBL:ACM21735.1};
GN   OrderedLocusNames=Geob_3392 {ECO:0000313|EMBL:ACM21735.1};
OS   Geotalea daltonii (strain DSM 22248 / JCM 15807 / FRC-32) (Geobacter
OS   daltonii).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=316067 {ECO:0000313|EMBL:ACM21735.1, ECO:0000313|Proteomes:UP000007721};
RN   [1] {ECO:0000313|EMBL:ACM21735.1, ECO:0000313|Proteomes:UP000007721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22248 / JCM 15807 / FRC-32
RC   {ECO:0000313|Proteomes:UP000007721};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C.,
RA   Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G.,
RA   Kostka J., Richardson P.;
RT   "Complete sequence of Geobacter sp. FRC-32.";
RL   Submitted (JAN-2009) 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; CP001390; ACM21735.1; -; Genomic_DNA.
DR   RefSeq; WP_012648463.1; NC_011979.1.
DR   AlphaFoldDB; B9M5H6; -.
DR   STRING; 316067.Geob_3392; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   KEGG; geo:Geob_3392; -.
DR   eggNOG; COG0457; Bacteria.
DR   eggNOG; COG0741; Bacteria.
DR   eggNOG; COG1729; Bacteria.
DR   HOGENOM; CLU_013746_0_0_7; -.
DR   OrthoDB; 9781970at2; -.
DR   Proteomes; UP000007721; Chromosome.
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; 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; PF13432; TPR_16; 3.
DR   Pfam; PF13174; TPR_6; 3.
DR   SMART; SM00028; TPR; 4.
DR   SUPFAM; SSF48435; Bacterial muramidases; 1.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   SUPFAM; SSF48452; TPR-like; 1.
DR   PROSITE; PS50005; TPR; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007721};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   TPR repeat {ECO:0000256|PROSITE-ProRule:PRU00339}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..717
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002888720"
FT   REPEAT          225..258
FT                   /note="TPR"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00339"
FT   DOMAIN          549..658
FT                   /note="Transglycosylase SLT"
FT                   /evidence="ECO:0000259|Pfam:PF01464"
SQ   SEQUENCE   717 AA;  79419 MW;  97653BF2C4FE5B98 CRC64;
     MLFRSLTALA LIILFSISAS GTTLFPLPDE ALQEASKHFR DKDYGPARES ALKAPQSGIR
     DFILGMAAIK LEQWQEAISY LGYAAHNFPL LGDYALYNQA TAFSRQDKHP EALASLGKML
     KVYPESPINR AAIYLKGNEL YASGNFIDAL KTYTDFIERY PQGADSLTAL YRSALCREQL
     GDPAAAASIL RSIPINYPAS SLTPKASLDL ERLAQTGIKI EPLSTNEIFR QGTILFDLGK
     YAQAIKTFDS VLQKSSNPEI NVRFQFKKAQ ALFKSRHYKD AEQLFTALGK VNSGKVLNGE
     IRFWLARTLA KNGKEDEAVS AYLLLADTWP KAALADDALL EAAQIRKSQK KTDEAQQLLQ
     RSLFLYPESG LKKSLLWEIA WERYQAKDYK AASDWFGKLA GYENARDRAL YWRGKSLAAA
     GDQEGAKASF SQLMTEFPLG YYALTHAKEA GIASTETTLP PVDLTEALPV PAGFERVKAL
     ITLGFYDEAQ KELSGQKKPK MQQGIARLYL EMGNYNAVVH LFKKEPLSRL DKESALAWGL
     NYPLAFRDYV TKNAGDSNLP ESLVYAIIRA ESTYSPTALS PVGAVGLMQL MPATASAVAR
     GKLDRNSLTV PAVNIRFGSK HLKDLLDYHN GDLVKVIAAY NAGSGNVGKW EKRLGDMPRD
     QFIENIPFGE TREYVKKVLA GMELYQRFYG LDRKPVEKAA TPAEKTAAVQ SELQPAQ
//
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