ID D4I472_ERWAC Unreviewed; 441 AA.
AC D4I472;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Uncharacterized metalloprotease yebA {ECO:0000313|EMBL:CBA21009.1};
DE EC=3.4.24.- {ECO:0000313|EMBL:CBA21009.1};
GN Name=yebA {ECO:0000313|EMBL:CBA21009.1};
GN OrderedLocusNames=EAMY_2059 {ECO:0000313|EMBL:CBA21009.1};
OS Erwinia amylovora (strain CFBP1430).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=665029 {ECO:0000313|EMBL:CBA21009.1, ECO:0000313|Proteomes:UP000001841};
RN [1] {ECO:0000313|EMBL:CBA21009.1, ECO:0000313|Proteomes:UP000001841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFBP1430 {ECO:0000313|Proteomes:UP000001841};
RX PubMed=20192826; DOI=10.1094/MPMI-23-4-0384;
RA Smits T.H., Rezzonico F., Kamber T., Blom J., Goesmann A., Frey J.E.,
RA Duffy B.;
RT "Complete genome sequence of the fire blight pathogen Erwinia amylovora
RT CFBP 1430 and comparison to other Erwinia spp.";
RL Mol. Plant Microbe Interact. 23:384-393(2010).
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}.
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DR EMBL; FN434113; CBA21009.1; -; Genomic_DNA.
DR RefSeq; WP_004157954.1; NC_013961.1.
DR AlphaFoldDB; D4I472; -.
DR STRING; 665029.EAMY_2059; -.
DR MEROPS; M23.011; -.
DR GeneID; 8911726; -.
DR KEGG; eam:EAMY_2059; -.
DR PATRIC; fig|665029.3.peg.1976; -.
DR eggNOG; COG0739; Bacteria.
DR HOGENOM; CLU_026846_0_2_6; -.
DR OrthoDB; 9805070at2; -.
DR Proteomes; UP000001841; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042834; F:peptidoglycan binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR013731; OapA_N.
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; PF08525; OapA_N; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SMART; SM00257; LysM; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CBA21009.1};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000313|EMBL:CBA21009.1};
KW Protease {ECO:0000313|EMBL:CBA21009.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT TRANSMEM 21..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..143
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 66..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..87
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 441 AA; 49007 MW; 304CAA4B9B3C5309 CRC64;
MQQKLNAISV AFNGLSRPHR ILLGALSVVT LAVAVWRPYV YHPGSESQIV KRVEVNQDQL
RTLLPEASEP IDGDSPAPED EVPNDEIDRD APNESGTHDY VVSGGDTLSS VLNQYGIDMS
DISKLVKTDR ELRNLQIGQQ LSWTLNGDGQ LQRMTWEVSR RESRTYDRAG DTFTLSSALK
SGEWQNHVLN GVVNGSFVNS AKSAGLSSGE VSAVIKSMQW QMDFRKLRDG DRFAVLTSRE
MLEGKSQQSQ LLGVRVNSGG KDYYAIRAED GKFYDRSGSG LSRGFMRFPT VKQYRVSSNF
NPRRTNPVTG RIAPHKGVDF AVPVGTPVLA IGDGEVIFSK RSGAAGNYVA IRHGRQYMTR
YMHLKTLLVK PGQKVKRGDR IALSGNTGRS TGPHVHFEVW INNQAVNPLT ARLPRMEGLS
GKERRDYLAQ VREVIPQLRI R
//
