ID W0HPY4_9GAMM Unreviewed; 441 AA.
AC W0HPY4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Cell wall endopeptidase family M23/M37 {ECO:0000313|EMBL:AHF74280.1};
GN Name=yebA {ECO:0000313|EMBL:AHF74280.1};
GN ORFNames=SOPEG_2619 {ECO:0000313|EMBL:AHF74280.1};
OS Candidatus Sodalis pierantonius str. SOPE.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Bruguierivoracaceae; Sodalis.
OX NCBI_TaxID=2342 {ECO:0000313|EMBL:AHF74280.1, ECO:0000313|Proteomes:UP000019025};
RN [1] {ECO:0000313|EMBL:AHF74280.1, ECO:0000313|Proteomes:UP000019025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=none {ECO:0000313|Proteomes:UP000019025};
RX PubMed=24407854; DOI=10.1093/gbe/evt210;
RA Oakeson K.F., Gil R., Clayton A.L., Dunn D.M., von Niederhausern A.C.,
RA Hamil C., Aoyagi A., Duval B., Baca A., Silva F.J., Vallier A.,
RA Jackson D.G., Latorre A., Weiss R.B., Heddi A., Moya A., Dale C.;
RT "Genome degeneration and adaptation in a nascent stage of symbiosis.";
RL Genome Biol. Evol. 6:76-93(2014).
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; CP006568; AHF74280.1; -; Genomic_DNA.
DR RefSeq; WP_025245821.1; NZ_CP006568.1.
DR AlphaFoldDB; W0HPY4; -.
DR STRING; 2342.SOPEG_2619; -.
DR KEGG; pes:SOPEG_2619; -.
DR PATRIC; fig|2342.5.peg.2792; -.
DR eggNOG; COG0739; Bacteria.
DR HOGENOM; CLU_026846_0_2_6; -.
DR Proteomes; UP000019025; Chromosome.
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; IPR013731; OapA_N.
DR InterPro; IPR007340; Opacity-associatedA.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF270; 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 SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000019025};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 98..143
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
FT REGION 62..95
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; 49086 MW; 2D8EF7C66950F49A CRC64;
MQQIARSFAL AFNHLPRPHR VMLGSLTIVT LAVAVWRPYI YSPVVERPAS RIIPLEDHQL
RELTPEASEP LDQTTPDSDE DIPKDELDER GEGEAGVHEY VISTGDTLSS VLTQYGIDIA
DVTALAQQNP ALRSLKIGQS LSWTLTAEGD LQRLTWDVSR RETRTYDRVN GGFKESIANM
TGEWRNTTLT GQLNGSFVTS VRAAGLTGSD INAVIKALQW QLDFRKLRKG DQFSVLTSRE
MLDGKSAQSQ LLGVRLRTGG KDYYAFRADD GKFYNRDAAG LARGFMRFPT VKQFRVSSNF
NPRRLNPVTG RIAPHRGVDF AVPVGTPVLA VGDGEVMVSK RDGAAGNYVA IRHGRQYMTR
YMHLKKLLVK SGQKVKRGDR IALSGNTGRS TGPHLHYEVW INQQAVNPLT AKLPRTEELT
GSDRAEYLAQ VKQMLPQLQL N
//