ID F4CAR8_SPHS2 Unreviewed; 297 AA.
AC F4CAR8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Peptidoglycan hydrolase {ECO:0000256|ARBA:ARBA00032108};
GN OrderedLocusNames=Sph21_0767 {ECO:0000313|EMBL:ADZ77344.1};
OS Sphingobacterium sp. (strain 21).
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Sphingobacterium.
OX NCBI_TaxID=743722 {ECO:0000313|EMBL:ADZ77344.1};
RN [1] {ECO:0000313|EMBL:ADZ77344.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=21 {ECO:0000313|EMBL:ADZ77344.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pagani I., Siebers A.K.,
RA Allgaier M., Thelen M.P., Hugenholtz P., Woyke T.;
RT "Complete sequence of Sphingobacterium sp. 21.";
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP002584; ADZ77344.1; -; Genomic_DNA.
DR AlphaFoldDB; F4CAR8; -.
DR STRING; 743722.Sph21_0767; -.
DR KEGG; shg:Sph21_0767; -.
DR PATRIC; fig|743722.3.peg.822; -.
DR eggNOG; COG1388; Bacteria.
DR eggNOG; COG1705; Bacteria.
DR HOGENOM; CLU_013771_1_0_10; -.
DR OrthoDB; 977752at2; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004040; F:amidase activity; IEA:InterPro.
DR GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR GO; GO:0031640; P:killing of cells of another organism; IEA:UniProtKB-KW.
DR GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR CDD; cd00118; LysM; 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; IPR002901; MGlyc_endo_b_GlcNAc-like_dom.
DR PANTHER; PTHR33308; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR PANTHER; PTHR33308:SF9; PEPTIDOGLYCAN HYDROLASE FLGJ; 1.
DR Pfam; PF01832; Glucosaminidase; 1.
DR Pfam; PF01476; LysM; 1.
DR SMART; SM00257; LysM; 1.
DR SMART; SM00047; LYZ2; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Antimicrobial {ECO:0000256|ARBA:ARBA00022638};
KW Bacteriolytic enzyme {ECO:0000256|ARBA:ARBA00022638};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..30
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 252..295
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 40..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 297 AA; 33761 MW; 247B60863036C2B0 CRC64;
MNKQPQHIAL PSFVYLILFF CISLSLTSCL PKQKVLQSSK TRQQGSYGSN NEGRRHHHPH
RPSNKPAAIS ASAQDYISRY KTIAIQEMNT YGIPASITLA QGLLESANGN STLAREANNH
FGIKCTPDWK GESFFKDDDA INDCFRVYRS PEDSFRDHSE FLLRKRYAPL FELDKDDYTG
WAKGLKKAGY ATNPHYAELL IDLIERYGLY EYDRGEKAPE KINREERVLV EIADNSPKEP
EKAEAKPPVE MKIHEVRQGD TIYSISKRYG LTTDELKNLN SLDSDDLVVG QLLLVSK
//
