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Database: UniProt
Entry: A0A2R3Z3K8_9FLAO
LinkDB: A0A2R3Z3K8_9FLAO
Original site: A0A2R3Z3K8_9FLAO 
ID   A0A2R3Z3K8_9FLAO        Unreviewed;       528 AA.
AC   A0A2R3Z3K8;
DT   20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT   20-JUN-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Lytic transglycosylase {ECO:0000313|EMBL:AVR44845.1};
GN   ORFNames=C7S20_05955 {ECO:0000313|EMBL:AVR44845.1};
OS   Christiangramia fulva.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Christiangramia.
OX   NCBI_TaxID=2126553 {ECO:0000313|EMBL:AVR44845.1, ECO:0000313|Proteomes:UP000241507};
RN   [1] {ECO:0000313|Proteomes:UP000241507}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SH35 {ECO:0000313|Proteomes:UP000241507};
RA   Hwang S.H., Hwang W.M., Kang K., Ahn T.-Y.;
RT   "Gramella fulva sp. nov., isolated from a dry surface of tidal flat.";
RL   Submitted (MAR-2018) 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; CP028136; AVR44845.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2R3Z3K8; -.
DR   KEGG; grs:C7S20_05955; -.
DR   OrthoDB; 9815002at2; -.
DR   Proteomes; UP000241507; Chromosome.
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; 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; 2.
DR   SUPFAM; SSF54106; LysM domain; 2.
DR   SUPFAM; SSF53955; Lysozyme-like; 1.
DR   PROSITE; PS51782; LYSM; 2.
DR   PROSITE; PS00922; TRANSGLYCOSYLASE; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000241507};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..528
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015360869"
FT   DOMAIN          414..457
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   DOMAIN          481..525
FT                   /note="LysM"
FT                   /evidence="ECO:0000259|PROSITE:PS51782"
FT   REGION          465..485
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   528 AA;  60584 MW;  276803730D29CAB5 CRC64;
     MLKQSLCIVF LLAGISIFAQ EKKNNERLEK ANFRVQIFKK TNNSEIKLAK PDPEFRDKLP
     ISAQIGDSSR IVLKDLPRAA SIDSLWRKEL TNSDLFERMQ RNIQDQDYEE VVYDALPTDT
     LKARLAKLNA RTPFNIEYNP ILESVIKSYL KRDKQNLERL MALSTYYFPL FEQELDKYDI
     PLEIKYLAII ESALNPRAKS RVGATGLWQF MFTTGKMHGL DVSSYVDERM DPARATEAAA
     EYLASLYKVF GDWDLVLASY NSGPGNVSKA IRRSGGSTDY WTLRRYLPRE TAGYVPAFLA
     TLYLFEYAQE HHFQPKNPDI VFFETDTIQV KQLLTFDQIS KVTGVDKSML EFLNPSYKLD
     IIPYVEDEKY VVRLPRPATG KFVNNEDAIY NFAEKDLANS EKELPKYVET EDRIRYRVKP
     GDYLGRIAER YGVGVSSLRN WNNLRSNNIR VGQYLTIYPR KPVTGQVASG NQKSSNKSDP
     KTYTVKQGDS LWSISRKFPG VTVQNLQSWN DVNSNSLKPG MKLKVSRG
//
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