ID A0A0H3GIW3_KLEPH Unreviewed; 645 AA.
AC A0A0H3GIW3;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=peptidoglycan lytic exotransglycosylase {ECO:0000256|ARBA:ARBA00012587};
DE EC=4.2.2.n1 {ECO:0000256|ARBA:ARBA00012587};
GN OrderedLocusNames=KPHS_07000 {ECO:0000313|EMBL:AEW59398.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW59398.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW59398.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW59398.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(2012).
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 Evidence={ECO:0000256|ARBA:ARBA00001420};
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; CP003200; AEW59398.1; -; Genomic_DNA.
DR RefSeq; WP_002887806.1; NC_016845.1.
DR RefSeq; YP_005225000.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GIW3; -.
DR STRING; 1125630.KPHS_07000; -.
DR GeneID; 11845690; -.
DR KEGG; kpm:KPHS_07000; -.
DR PATRIC; fig|1125630.4.peg.680; -.
DR HOGENOM; CLU_019016_1_1_6; -.
DR Proteomes; UP000007841; 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:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; 1.25.20.10; Bacterial muramidases; 1.
DR Gene3D; 1.10.1240.20; Lytic transglycosylase, superhelical linker domain; 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 PANTHER; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR Pfam; PF01464; SLT; 1.
DR Pfam; PF14718; SLT_L; 1.
DR SUPFAM; SSF48435; Bacterial muramidases; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..27
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 28..645
FT /note="peptidoglycan lytic exotransglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002610150"
FT DOMAIN 407..472
FT /note="Lytic transglycosylase superhelical linker"
FT /evidence="ECO:0000259|Pfam:PF14718"
FT DOMAIN 486..596
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 645 AA; 73160 MW; 5990FF1985AF2D6C CRC64;
MEKAKKMTWH LLAASVGLLT LSQLAHADSL DEQRSRYAQI KQAWDNRQMD VVDQLMPTLS
TYPLYPYLQY RQITDDLMNQ PALVVKNFID ANPTLPPARS LRSRFVNELA RRSDWRGLLA
FSPDKPTSTE AQCNYYYAKL SVGQSQEAWS GAKELWLTGK NQPGACEPLF SAWRDSGQQD
PLAYLERIRL AMKAGNIGLV KSLAQQMPAN YQSIASAVVA LANDPNSVLT FARTTGATDF
TRQMAAVAFA SVARQDVENA RLMIPSLVQA QQLNEDQTQE LRDIVAWRLM GSDVTEEQAI
WRDDAIMRSQ STPLVERRVR MALGTGDRHG LNTWLARLPM EAKEKDEWRY WQADLLLERG
RDEEAQAILR SLMQQRGFYP MVAAQRLGEE YTFRIDKASG TIDPALASGP EMARVRELMY
WNMDNTARTE WANLVTSRTK SQQAQLARYA FDQHWWDLSV QATIAGKLWD QLEERFPLAY
NDLFARYVSG KDIPQSYAMA IARQESAWNP KVRSPVGASG LMQIMPGTAT HTVSMFSIPG
YSGPSQLLDP ETNINIGTSY LQYVYQQFGN NRIYASAAYN AGPGRVRSWQ GNSAGRIDAV
AFVESIPFSE TRGYVKNVLS YDAYYRYFMG QQDKILSDAE WRQRY
//
