ID   SLT_HAEIN               Reviewed;         593 AA.
AC   P44888;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=Putative soluble lytic murein transglycosylase;
DE            EC=4.2.2.n1;
DE   AltName: Full=Peptidoglycan lytic exotransglycosylase;
DE   Flags: Precursor;
GN   Name=slt; OrderedLocusNames=HI_0829;
OS   Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=71421;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX   PubMed=7542800; DOI=10.1126/science.7542800;
RA   Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA   Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA   McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA   Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA   Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA   Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA   Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA   Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT   "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT   Rd.";
RL   Science 269:496-512(1995).
CC   -!- FUNCTION: Murein-degrading enzyme. May play a role in recycling of
CC       muropeptides during cell elongation and/or cell division (By
CC       similarity). {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Exolytic cleavage of the (1->4)-beta-glycosidic linkage
CC         between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine
CC         (GlcNAc) residues in peptidoglycan, from either the reducing or the
CC         non-reducing ends of the peptidoglycan chains, with concomitant
CC         formation of a 1,6-anhydrobond in the MurNAc residue.; EC=4.2.2.n1;
CC   -!- SUBCELLULAR LOCATION: Periplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family. {ECO:0000305}.
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DR   EMBL; L42023; AAC22487.1; -; Genomic_DNA.
DR   PIR; C64097; C64097.
DR   RefSeq; NP_438989.1; NC_000907.1.
DR   RefSeq; WP_010869063.1; NC_000907.1.
DR   AlphaFoldDB; P44888; -.
DR   SMR; P44888; -.
DR   STRING; 71421.HI_0829; -.
DR   CAZy; GH23; Glycoside Hydrolase Family 23.
DR   PRIDE; P44888; -.
DR   EnsemblBacteria; AAC22487; AAC22487; HI_0829.
DR   KEGG; hin:HI_0829; -.
DR   PATRIC; fig|71421.8.peg.870; -.
DR   eggNOG; COG0741; Bacteria.
DR   HOGENOM; CLU_019016_1_0_6; -.
DR   OMA; QWFELAV; -.
DR   PhylomeDB; P44888; -.
DR   BioCyc; HINF71421:G1GJ1-870-MON; -.
DR   Proteomes; UP000000579; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR   Gene3D; 1.10.1240.20; -; 1.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   InterPro; IPR037061; Lytic_TGlycoase_superhlx_L_sf.
DR   InterPro; IPR012289; Lytic_TGlycosylase_superhlx_L.
DR   InterPro; IPR008939; Lytic_TGlycosylase_superhlx_U.
DR   InterPro; IPR000189; Transglyc_AS.
DR   InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR   Pfam; PF01464; SLT; 1.
DR   Pfam; PF14718; SLT_L; 1.
DR   SUPFAM; SSF48435; SSF48435; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Cell wall biogenesis/degradation; Lyase; Periplasm; Reference proteome;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..593
FT                   /note="Putative soluble lytic murein transglycosylase"
FT                   /id="PRO_0000032780"
FT   REGION          152..176
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..529
FT                   /note="Slt-type domain"
FT   ACT_SITE        453
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   593 AA;  68691 MW;  774DDD3D38217CEE CRC64;
     MKKVALISLC IFTALSAFAD SPNTATASIN LEQEKQNWEL AQHQDYLKRL KQREVFLQVE
     GLLKSAVKKQ QFSEATQNIT KTLIDSLQGY PLQYDLLARF WETKIAFLQN DDIQGRQQAI
     NELNALVQQN YPFVTPAFQA LLQKLSTLNE QQTSATSDNA KENNRVQKEQ NQVENPKQLA
     EIVRKSDPNT LDKTVLIDAF PRYLKTLPEQ MNNLSFESYQ KWANTWQLSE DEIKQWKIAF
     LNRFFDNENT DFQKWRDEQI RQLQTDNLTE RRLRMAIWQK TELTSWLNLL SAESKSKQEW
     RYWEAKQDIL KNTKKLTALS KERGFYPMLA ATQLKQAYQL NVPIAPSFTQ AEQLPFKQVF
     AMITELRELG RNGLAKQRWR ILLDNVDFTT QLKLSEYAKN QQWFELAVDA SIVAKAWDYL
     SLRLPNAYSE YFNAALQNLN ISKTFAMAIA RQESAWNPMA QSSANARGLM QLLPSTAKLT
     AENNQLPYQG EQDLFKPLNN ILLGTAHLNE LNGKYPNNRI LIAAAYNAGA NRVGKWLSRA
     SGKLALDEFV ASIPFYETRG YVQNVVAYDF YYQILQNKEN PQIFSQEELN RLY