ID A0A179DKX4_9SPHI Unreviewed; 469 AA.
AC A0A179DKX4;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:OAQ41618.1};
GN ORFNames=A5893_00465 {ECO:0000313|EMBL:OAQ41618.1};
OS Pedobacter psychrophilus.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Pedobacter.
OX NCBI_TaxID=1826909 {ECO:0000313|EMBL:OAQ41618.1, ECO:0000313|Proteomes:UP000078459};
RN [1] {ECO:0000313|EMBL:OAQ41618.1, ECO:0000313|Proteomes:UP000078459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ41618.1,
RC ECO:0000313|Proteomes:UP000078459};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OAQ41618.1, ECO:0000313|Proteomes:UP000078459}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCM 8644 {ECO:0000313|EMBL:OAQ41618.1,
RC ECO:0000313|Proteomes:UP000078459};
RA Svec P.;
RT "Pedobacter psychrophilus sp. nov., isolated from Antarctic fragmentary
RT rock.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
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:OAQ41618.1}.
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DR EMBL; LWHJ01000011; OAQ41618.1; -; Genomic_DNA.
DR RefSeq; WP_068820649.1; NZ_LWHJ01000011.1.
DR AlphaFoldDB; A0A179DKX4; -.
DR STRING; 1826909.A5893_00465; -.
DR OrthoDB; 9815002at2; -.
DR Proteomes; UP000078459; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0008933; F:lytic transglycosylase activity; IEA:InterPro.
DR GO; GO:0000270; P:peptidoglycan metabolic process; IEA:InterPro.
DR CDD; cd00118; LysM; 2.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 2.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR023346; Lysozyme-like_dom_sf.
DR InterPro; IPR000189; Transglyc_AS.
DR InterPro; IPR008258; Transglycosylase_SLT_dom_1.
DR PANTHER; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR PANTHER; PTHR33734:SF22; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D; 1.
DR Pfam; PF01476; LysM; 2.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 2.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000078459}.
FT DOMAIN 362..405
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 423..467
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 469 AA; 53339 MW; 65C883DC9D2716E6 CRC64;
MKKTIALITS IILLISLSIS AKEKFKLDTT KKIKLSAKEA KLIKNLIKTD TIFDPANLNL
QLELFKYNPN LIYKYRLDSL NATVPMDYNS YVQTYIDVFL TKRNEEVGHM INLGKYYFPI
FEKALAAYHV PQEFKYLPII ESSMNPMAVS RVGATGMWQF MYTTGRVYGL NIDNYVDDRK
DPIAASYAAA AYLRDSYNEL GDWLLALASY NCGKGNVTRA ISKAGGARSF WEIQGYLPNE
TRNYVPAFIA ANYIMNYYGK HSQIKLINEN ILKTDSVYVN KFISFDKIAS ALNLEANDIQ
NLNPSYKKLL INGTKENPKR LIIPKLTYTD YTNFFDALNA DEDESIKIVN VIQQPTKPFK
TITHTVKQGE NLNRIADNYR VEVQDIKVWN NLPNYTISIG QKLVVNKPIE EVKKPIEKKS
DLLAYKVKAG DTLISIAERF ENVTVQSIKE LNGLKSSILT IGAILKIKI
//
