ID A0A259FNL6_9PROT Unreviewed; 516 AA.
AC A0A259FNL6;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:OZA40193.1};
GN ORFNames=B7X87_01010 {ECO:0000313|EMBL:OZA40193.1};
OS Hydrogenophilales bacterium 17-64-34.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970527 {ECO:0000313|EMBL:OZA40193.1, ECO:0000313|Proteomes:UP000216129};
RN [1] {ECO:0000313|EMBL:OZA40193.1, ECO:0000313|Proteomes:UP000216129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-64-34 {ECO:0000313|EMBL:OZA40193.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) 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:OZA40193.1}.
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DR EMBL; NCIL01000001; OZA40193.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259FNL6; -.
DR Proteomes; UP000216129; 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; IPR001387; Cro/C1-type_HTH.
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; 3.
DR SUPFAM; SSF54106; LysM domain; 2.
DR SUPFAM; SSF53955; Lysozyme-like; 1.
DR PROSITE; PS50943; HTH_CROC1; 1.
DR PROSITE; PS51782; LYSM; 2.
DR PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE 3: Inferred from homology;
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..34
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 35..516
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012582057"
FT DOMAIN 397..441
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT DOMAIN 405..421
FT /note="HTH cro/C1-type"
FT /evidence="ECO:0000259|PROSITE:PS50943"
FT DOMAIN 468..513
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 516 AA; 56174 MW; CBF46E9A1F22A5A9 CRC64;
MKPHRVRDSV LLRSPLARLG LACCLAGLAQ ATLAAETLAG IQSLQWQPDI PVVADAAPQA
LGDVWSRIRE GFKIDDAADA NPLVARHVAW YAARPDYLRR MTERSRRYLY HIVQEVERRA
MPMEIALLPM IESAFNPTAL SPSAASGIWQ FIPSTGRLYG LRQDTWYDGR RDFTEATRAA
LDYLGKLYLD FGDWQLALAA YNCGEGCVAR AIQKNVALGL PTDYASLSLP TETRHYVPKL
LAVRQMVRSP ESFGIALSPL ANEPYFDEVT VHASLDVQSA ARLAGVSHDE FLALNAAFPK
KLIRSDAPVR LLVPAGRGET FERNLEAGDW DSWQPYTAPR GERPEAIARR LGVSLDRLQA
HNQFHLKRGK FTHAQTILVP VKGSLSQPAE TSPVSADGYS VQPGDTLFRI ARAYGVSVDE
IMAVNPSLTG DALRPGQVLS LPAGSQAGLA PARIQPASLA SGPAKSPRTY TVKRGDTLHA
IARQFGIQLA EIHAGNPGLR GSAAIHPGLR ITLPAR
//
