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Database: UniProt
Entry: A0A1H4FPV5_9GAMM
LinkDB: A0A1H4FPV5_9GAMM
Original site: A0A1H4FPV5_9GAMM 
ID   A0A1H4FPV5_9GAMM        Unreviewed;       409 AA.
AC   A0A1H4FPV5;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Membrane-bound lytic murein transglycosylase D {ECO:0000313|EMBL:SEA99346.1};
GN   ORFNames=SAMN05660964_03070 {ECO:0000313|EMBL:SEA99346.1};
OS   Thiothrix caldifontis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiothrix.
OX   NCBI_TaxID=525918 {ECO:0000313|EMBL:SEA99346.1, ECO:0000313|Proteomes:UP000199397};
RN   [1] {ECO:0000313|EMBL:SEA99346.1, ECO:0000313|Proteomes:UP000199397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21228 {ECO:0000313|EMBL:SEA99346.1,
RC   ECO:0000313|Proteomes:UP000199397};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the transglycosylase Slt family.
CC       {ECO:0000256|ARBA:ARBA00007734}.
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DR   EMBL; FNQP01000023; SEA99346.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H4FPV5; -.
DR   STRING; 525918.SAMN05660964_03070; -.
DR   Proteomes; UP000199397; 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; PTHR33734; LYSM DOMAIN-CONTAINING GPI-ANCHORED PROTEIN 2; 1.
DR   PANTHER; PTHR33734:SF22; MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE D; 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   Reference proteome {ECO:0000313|Proteomes:UP000199397}.
FT   DOMAIN          355..398
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..40
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   409 AA;  45787 MW;  E6394A9ECCD2C29B CRC64;
     MGKPEQASKQ PTLRKASLHS TSLANDAQTS TQQQAQQKPV LDNDFDTWER VFRGFKLNNQ
     YSQHPQVQRF VQYYGRNPAQ LSLLSERASV FLHMIVHEVE RRDMPNELAL LPFVESAFDA
     DVFSHAGAAG LWQFIPDTGR RYGLQQARSY DARMDPFAAT GAALTYLQKL NNDFNGDWLL
     ALAAYNCGEN RVQREIDRNR AKGLPTTFWH LSLPKETREY VPRLLAFKEL IGNAPRYGIT
     LPETPNSARL AQLRIDKPVD LRQAALQAGL AADTLLNLNP CFRTGITTPQ YSNRIVLPRQ
     YAKQLVQAIE ALPPAANNRI YASKSSSGYN KLATTRMGKK KSSQLAKAKT KSSVKVHTVR
     RGDTLQSIAL RHGTTVKTLM KHNSKRTSKL KVGERLDVIA SVSGVNVQS
//
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