ID A0A095TVN8_9GAMM Unreviewed; 637 AA.
AC A0A095TVN8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:KGD66463.1};
GN ORFNames=Y5S_00130 {ECO:0000313|EMBL:KGD66463.1};
OS Alcanivorax nanhaiticus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=1177154 {ECO:0000313|EMBL:KGD66463.1, ECO:0000313|Proteomes:UP000029444};
RN [1] {ECO:0000313|EMBL:KGD66463.1, ECO:0000313|Proteomes:UP000029444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=19-m-6 {ECO:0000313|EMBL:KGD66463.1,
RC ECO:0000313|Proteomes:UP000029444};
RA Lai Q., Shao Z.;
RT "Genome Sequence of alkane-degrading Bacterium Alcanivorax sp. 19-m-6.";
RL Submitted (SEP-2012) 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:KGD66463.1}.
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DR EMBL; ARXV01000001; KGD66463.1; -; Genomic_DNA.
DR RefSeq; WP_035229387.1; NZ_ARXV01000001.1.
DR AlphaFoldDB; A0A095TVN8; -.
DR STRING; 1177154.Y5S_00130; -.
DR PATRIC; fig|1177154.3.peg.131; -.
DR eggNOG; COG0741; Bacteria.
DR OrthoDB; 92254at2; -.
DR Proteomes; UP000029444; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..637
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001909977"
FT DOMAIN 393..455
FT /note="Lytic transglycosylase superhelical linker"
FT /evidence="ECO:0000259|Pfam:PF14718"
FT DOMAIN 467..578
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 637 AA; 73039 MW; 6B180A797CB8BB74 CRC64;
MVRAAVLIAC SLMAPLAMAD TSTFRQALDA ARNDDWETLS RMESALDDNH PLEAYLEFHR
IRVGLPELPP EKIQAYAETY SDSPLPGDVV DMAIVAYGKA KRWDALLTVS ETAPREVALQ
CYYYQAKLAN NDESALQEAA RLWAHGSSRP NACDPLFDAA RQAGVIDDKA IWERQRLAFE
AGNYSLMRYL NRLLEGSDYE TAGNWLKKLY RSPDSLSDLP RGLSGEQKEM LREAGLFRWI
YTDTIAARKW FEKQATQITN DDARESLGRR LAWYSTIRGI EENRAWLDQW LESHSDVELL
SQRARRAVIE QNWEATAHWI RKLPAEEQAD SRWRYWLSRA LEATGEEDTA RELLQQAAKG
RNFFAFLAAD RLGEPYRFSD APYSATVDFK APKAVNRIVL LQELEEDTAA HREWLWLLWH
SDREQQRALA DYALKKQWYS LAVEASIQSK SWDTLAWRFP PAYRAQFEKE GVENDLDPWL
AMSVSRRESA FNPRARSGVG ASGLMQLMPA TARQVAKEAN QERPTQAMLF DQNVNIGLGT
RYLAELLEQF NGNRLLALAA YNAGPHRIDN WLEEEDDKAV PADVWVESIP FRETRDYVQA
VLTYRVLFIG LHDDQPRTAQ LMTDMESESR YSLSMLE
//
