ID A0A0F5ANV5_9GAMM Unreviewed; 668 AA.
AC A0A0F5ANV5;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:KKA44332.1};
GN ORFNames=WN56_11575 {ECO:0000313|EMBL:KKA44332.1};
OS Salinivibrio sp. KP-1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Salinivibrio.
OX NCBI_TaxID=1406902 {ECO:0000313|EMBL:KKA44332.1, ECO:0000313|Proteomes:UP000033449};
RN [1] {ECO:0000313|EMBL:KKA44332.1, ECO:0000313|Proteomes:UP000033449}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KP-1 {ECO:0000313|EMBL:KKA44332.1,
RC ECO:0000313|Proteomes:UP000033449};
RA Kaur G., Kumar A., Mathan Kumar R., Kumar N., Singh N.K., Arora A.,
RA Kaur N., Bala M., Mayilraj S.;
RT "Taxonomic description and genome sequence of Salinivibrio halophilus sp.
RT nov., a novel halotolerant gammaproteobacterium isolated from marine
RT sediment and emended description of the genus Salinivibrio.";
RL Submitted (MAR-2015) 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:KKA44332.1}.
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DR EMBL; LAQR01000041; KKA44332.1; -; Genomic_DNA.
DR RefSeq; WP_046075149.1; NZ_LAQR01000041.1.
DR AlphaFoldDB; A0A0F5ANV5; -.
DR PATRIC; fig|1406902.3.peg.2300; -.
DR Proteomes; UP000033449; Unassembled WGS sequence.
DR GO; GO:0042597; C:periplasmic space; IEA:InterPro.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; 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; 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.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000033449};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 435..496
FT /note="Lytic transglycosylase superhelical linker"
FT /evidence="ECO:0000259|Pfam:PF14718"
FT DOMAIN 513..619
FT /note="Transglycosylase SLT"
FT /evidence="ECO:0000259|Pfam:PF01464"
SQ SEQUENCE 668 AA; 77048 MW; 5A288ECABABF4DDB CRC64;
MERFIALSGP LRNASYAARR GVRAFSRSLL PGLILGAAFS PSLTLASASP DSGQMTPAQR
QYEAAIDAIE RGELRQFRRL KAKLRDYPLY PYLDYRDFTR NLAEKSHDSV TNFIQRYTTM
PFANSLRADY LSLLADRKDW ATLVAFQPDV PRGERYQCQY YYAHSQAGNR ALARSGAKSL
YLSGQSVDSA CDPLFDYLSE QKQLTGDLIL QRMLLTFEGR NRSLMRYLQG QLPDTHQATG
KQIIDLYDKP DQVADFSKRS KVTPFNQTLT RLAFERLARK DEAQAIRHFR RTVEGQHYDK
DERQAIADYL IGQLMNDDEP ALAAWRDRML RQSDDDGLLE RRFRLALVEG DWHVLNQWLS
LLSDEAKQSL KWRYWQARIQ LELGDSHAAN QAFETMLGER NFYSVAAAQH LEKPIHIPSR
TAVLKEAGLM PVNDVLARVD ELIALDKIYA AKREWYYVLQ RASDEQIALL AAYANKQHWY
HLAVQATIAG KMWDHLSLRF PLAHQWWFEF FSRERGVDKT TLMALSRQES AFFTRAVSHV
GARGLMQLMP RTARETSRRL GFDYQGPASL SDPGVNIRLG SGYLKMMLDR FDSNRVLAFA
AYNAGPHRVS RWLARSKGHM DAIAFIESIP FYETRHYVQN VLMFDIYYRQ LLGEPVQFLR
AHELAQRY
//
