ID U2IGP5_9PORP Unreviewed; 485 AA.
AC U2IGP5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE SubName: Full=Transglycosylase SLT domain protein {ECO:0000313|EMBL:ERJ73036.1};
GN ORFNames=HMPREF1556_00324 {ECO:0000313|EMBL:ERJ73036.1};
OS Porphyromonas sp. oral taxon 278 str. W7784.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1227272 {ECO:0000313|EMBL:ERJ73036.1, ECO:0000313|Proteomes:UP000016628};
RN [1] {ECO:0000313|EMBL:ERJ73036.1, ECO:0000313|Proteomes:UP000016628}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W7784 {ECO:0000313|EMBL:ERJ73036.1,
RC ECO:0000313|Proteomes:UP000016628};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Warren W., Mitreva M., Mardis E.R.,
RA Wilson R.K.;
RL Submitted (JUN-2013) 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:ERJ73036.1}.
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DR EMBL; AWUX01000025; ERJ73036.1; -; Genomic_DNA.
DR RefSeq; WP_021666667.1; NZ_KI259228.1.
DR AlphaFoldDB; U2IGP5; -.
DR STRING; 1227272.HMPREF1556_00324; -.
DR PATRIC; fig|1227272.3.peg.275; -.
DR eggNOG; COG0741; Bacteria.
DR eggNOG; COG1388; Bacteria.
DR HOGENOM; CLU_009520_1_0_10; -.
DR Proteomes; UP000016628; 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; 1.
DR CDD; cd16894; MltD-like; 1.
DR Gene3D; 1.10.530.10; -; 1.
DR Gene3D; 3.10.350.10; LysM domain; 1.
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; PTHR37423:SF2; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE; 1.
DR PANTHER; PTHR37423; SOLUBLE LYTIC MUREIN TRANSGLYCOSYLASE-RELATED; 1.
DR Pfam; PF01476; LysM; 1.
DR Pfam; PF01464; SLT; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..485
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004629652"
FT DOMAIN 417..460
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 379..424
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 442..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..413
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 460..474
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 485 AA; 54582 MW; 12CD8C18B8DD5CEB CRC64;
MKLLIKLLSI TALILVSVRT LPAQVDSVKR VDRPTSPFTL ASALLDPITL PASLDKDVER
MLEQWYSGYG NSTGGRQQSG RYSSVSVPYT PDSTYIRMLN RMPSAMRFSY NPLVREAIEL
YLFKRRGLLS SMLSLSDLYF PEIEMTLDKS GLPMELRYLV IVESALNPKA ISPAGAAGLW
QLMLPTGKIY GLTVNSLVDE RMDPVKSTEA ACRFLKDLYR IYGDWWLVLA AYNCGPGNVN
RALKRTGTDR PNFWEIYRYL PNETRRYIPL FIGAYFAMHY HREYGILPRQ LGRPLATDYY
TANHRVTFDR ISEITGLSTE LISTFNPQFR RGIIPGNTTP YPVRLPLSAI LKLDSAGSEV
HSPELRVNFD GPASVATTRS TVRAKAQQEE QEEATEEEDA KPSSRHGKRT TERQTTSTHA
VTSGETLYSL AHKYGTTVEE LRKNNNLRSD KLSVGQKIKI TKAAKSSGSS SRSSKATKRG
KKRRR
//
