ID I2JMX0_9GAMM Unreviewed; 645 AA.
AC I2JMX0;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Lytic transglycosylase catalytic subunit subunit {ECO:0000313|EMBL:EIF44322.1};
GN ORFNames=DOK_04362 {ECO:0000313|EMBL:EIF44322.1};
OS gamma proteobacterium BDW918.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Spongiibacteraceae.
OX NCBI_TaxID=1168065 {ECO:0000313|EMBL:EIF44322.1, ECO:0000313|Proteomes:UP000003473};
RN [1] {ECO:0000313|EMBL:EIF44322.1, ECO:0000313|Proteomes:UP000003473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BDW918 {ECO:0000313|EMBL:EIF44322.1,
RC ECO:0000313|Proteomes:UP000003473};
RX PubMed=22740675; DOI=10.1128/JB.00678-12;
RA Kim S.M., Cho S.J., Lee S.B.;
RT "Genome Sequence of the Unclassified Marine Gammaproteobacterium BDW918.";
RL J. Bacteriol. 194:3753-3754(2012).
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:EIF44322.1}.
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DR EMBL; AJMK01000021; EIF44322.1; -; Genomic_DNA.
DR AlphaFoldDB; I2JMX0; -.
DR PATRIC; fig|1168065.3.peg.917; -.
DR eggNOG; COG0741; Bacteria.
DR HOGENOM; CLU_019016_0_1_6; -.
DR Proteomes; UP000003473; Unassembled WGS sequence.
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; 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:UP000003473};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..645
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003661010"
FT DOMAIN 398..464
FT /note="Lytic transglycosylase superhelical linker"
FT /evidence="ECO:0000259|Pfam:PF14718"
FT DOMAIN 475..584
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 645 AA; 73586 MW; A4EDF68C320E8D6C CRC64;
MNRFFTLLVV LAIQATTVIA DPATDNSRRL YREALTEISR GRIANAEKLT PQLSNYALYP
YLELELLKAQ INQVSQQTID VYLQQYGDTI TGQRIRLTWL NKLLRNRNWT LYTQYYQKSS
SIQNRCHYAH ALRQIGKQSE ANVAVSELWS TPYSLPKECD TPIKEWLSTL SPAQTEQQYW
HRANLALSSG QTDMAFYLLS KVKGSDTYVE ILRNPNLLFS KGLTLSPNDR SRDIAVHTLK
RLAKGDFERT NTLWQQLDRQ LKFTPSQNYA LRDSMARQII ASDADYTRDW VMATDPNYED
PYLTEWRIRL ALKDGDWAAV QHIAQFLPED KKQKADWRYW AARADIELRG ELTVSTQLAL
QKLAAERGYY SFLAADILNE DYQLSASRTL DPALISEVEQ HSAIARAREL YLLGDTGTSN
LEWAYAMRSL NKAEQVAAAQ LALNWGWHYQ SIMTALKADA WDDLELRFPT PHQDNFRKVA
KREKIQLKWI YAIARQESAF APAANSPVGA RGLMQLMPGT AKLVAKQMGL PSPKTEDLLT
PEKNIAMGGF YLGQLLEQFG GNRILATAAY NAGPGRIERV LLRQTKDMPA DIWIENLPYG
ETREYIKNVL AFSVIYAAKL DLERPLLARE ERQIGPKNSA TALKN
//
