ID A0A0L7SX25_9GAMM Unreviewed; 419 AA.
AC A0A0L7SX25;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Peptidase {ECO:0000313|EMBL:KOC87640.1};
GN ORFNames=NG42_19660 {ECO:0000313|EMBL:KOC87640.1}, NG43_16765
GN {ECO:0000313|EMBL:KOC90779.1};
OS Winslowiella iniecta.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Winslowiella.
OX NCBI_TaxID=1560201 {ECO:0000313|EMBL:KOC87640.1, ECO:0000313|Proteomes:UP000037088};
RN [1] {ECO:0000313|Proteomes:UP000036851, ECO:0000313|Proteomes:UP000037088}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B120 {ECO:0000313|EMBL:KOC87640.1,
RC ECO:0000313|Proteomes:UP000037088}, and B149
RC {ECO:0000313|EMBL:KOC90779.1, ECO:0000313|Proteomes:UP000036851};
RX PubMed=26198254;
RA Campillo T., Luna E., Portier P., Fischer-Le Saux M., Lapitan N.,
RA Tisserat N.A., Leach J.E.;
RT "Erwinia iniecta sp. nov., isolated from Russian wheat aphids (Diuraphis
RT noxia).";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(2015).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase M23B family.
CC {ECO:0000256|ARBA:ARBA00006646}.
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:KOC87640.1}.
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DR EMBL; JRXE01000035; KOC87640.1; -; Genomic_DNA.
DR EMBL; JRXF01000028; KOC90779.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7SX25; -.
DR STRING; 1560201.NG42_19660; -.
DR PATRIC; fig|1560201.3.peg.4173; -.
DR Proteomes; UP000036851; Unassembled WGS sequence.
DR Proteomes; UP000037088; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR CDD; cd00118; LysM; 1.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 3.10.450.350; -; 2.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR045834; Csd3_N2.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR018392; LysM_dom.
DR InterPro; IPR036779; LysM_dom_sf.
DR InterPro; IPR007340; Opacity-associatedA.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF291; MUREIN DD-ENDOPEPTIDASE MEPM; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF19425; Csd3_N2; 1.
DR Pfam; PF04225; OapA; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR SUPFAM; SSF54106; LysM domain; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000037088};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 76..121
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 44..80
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 419 AA; 46743 MW; 92E0B9B07D1335A9 CRC64;
MLGSLTVVTL AVAVWRPYIY HPGENPIVKH IELDKSELRT LLPEASEPID QPTPAPEEDI
PKDEIDEDVP NESGTHDYTV STGDTLSSIL NQYGIDMSDI NQLANADKDL RNLKIGQQIS
WTLTDDGQLQ RMTWEMSRRE TRTYDRSGNG FKASSEMQQG EWKNSVLNGS LNGSFVSSAR
KAGLSSGEAS AVIKAMQWQM DFRKLRSGDQ FSVLMSREMM DGKSEQSHLL GVRMRTGGKD
YYAIRAEDGK FYDRSGSGLA RGFMRFPTVK QYRVSSNFNP RRLNPVTGRI APHKGVDFAI
PIGTPVLAVG DGEVVVAKRS GGAGNYVAIR HGRQYMTRYM HLKKLLVKPG EKVKRGDRIA
LSGNTGRSTG PHLHYEIWIN NQAVNPLTAK LPRSEGLTGQ DRKEYLAQVR DVVPQLRFD
//
