ID Q9CNU8_PASMU Unreviewed; 680 AA.
AC Q9CNU8;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 103.
DE RecName: Full=Lytic murein transglycosylase {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=PM0326 {ECO:0000313|EMBL:AAK02410.1};
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843 {ECO:0000313|EMBL:AAK02410.1, ECO:0000313|Proteomes:UP000000809};
RN [1] {ECO:0000313|EMBL:AAK02410.1, ECO:0000313|Proteomes:UP000000809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70 {ECO:0000313|EMBL:AAK02410.1,
RC ECO:0000313|Proteomes:UP000000809};
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
CC -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC {ECO:0000256|ARBA:ARBA00007734}.
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DR EMBL; AE004439; AAK02410.1; -; Genomic_DNA.
DR RefSeq; WP_010906589.1; NC_002663.1.
DR AlphaFoldDB; Q9CNU8; -.
DR STRING; 272843.PM0326; -.
DR CAZy; GH23; Glycoside Hydrolase Family 23.
DR EnsemblBacteria; AAK02410; AAK02410; PM0326.
DR KEGG; pmu:PM0326; -.
DR PATRIC; fig|272843.6.peg.339; -.
DR HOGENOM; CLU_019016_1_0_6; -.
DR OrthoDB; 92254at2; -.
DR Proteomes; UP000000809; 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; 1.25.20.10; 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; PF00760; Cucumo_coat; 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 Reference proteome {ECO:0000313|Proteomes:UP000000809};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..680
FT /note="Lytic murein transglycosylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004324482"
FT DOMAIN 443..508
FT /note="Lytic transglycosylase superhelical linker"
FT /evidence="ECO:0000259|Pfam:PF14718"
FT DOMAIN 525..631
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 680 AA; 78917 MW; 1B1732929E5C4A8C CRC64;
MKLTKIALTY LLTLMSMSLA AVSVSVPEDK TQPTEASLTT TNLVQARQIY QKIHQLLQRS
QSENTQRIVQ ALLAKIEDYP LYPYAQYAYL KALKDQLSLA QIEAFQTDFP SFPLTTELQK
QWLQQAQDKA EWQAIIHSPF RPKDMASRCI QLQAEYETQP NSPAFSLKQW QQQVAQIWRN
GASLPKACDT LFARWKEKGY PEETELKERA VLAFEQGNQA LLASLSQQAD QADTKRWLNE
LHQLSKNPLR LQHPQSAFFI DTLSADDPFA QRILLSHFST LIKRLKETDI KNQHDPFEPY
AQWANKLRLS EAQQRQWKKH LISHLFDSEN LNLQKWRDAQ LFELKEDTLT ERRLRTALRE
KTELTPWLDL LSNSAKQKEE WRFWQAKVFA QNKKTTEQAQ QIFQQLAKQR GFYPLLASAE
LNIDYAPAMD VFSSTSATDI HEKFSVELSR IAELREHNAT QYMNLEWKAL LEKANFEQKL
ALSQFATEQA WFDLGVEATI QAKAWGYLAL RLPNAYLDWF DLHLNNKNVS RTFAMAIARQ
ESAWKPYVSS HANAQGLMQL LPSTAKQTAQ EAGLPYTHQK QLFDPFDNIM LGTAHLQQLY
DKYGNNRILI AAAYNAGASR VDRWLAKADG KLSMAEFIAS IPFYETRGYV QNVLTYDVYY
QWLQQQPQQK FSQDEYNRLY
//