ID A1AV70_RUTMC Unreviewed; 372 AA.
AC A1AV70;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 76.
DE SubName: Full=Peptidase M23B {ECO:0000313|EMBL:ABL01827.1};
GN OrderedLocusNames=Rmag_0024 {ECO:0000313|EMBL:ABL01827.1};
OS Ruthia magnifica subsp. Calyptogena magnifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; sulfur-oxidizing symbionts;
OC Candidatus Ruthturnera.
OX NCBI_TaxID=413404 {ECO:0000313|EMBL:ABL01827.1, ECO:0000313|Proteomes:UP000002587};
RN [1] {ECO:0000313|EMBL:ABL01827.1, ECO:0000313|Proteomes:UP000002587}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cm {ECO:0000313|EMBL:ABL01827.1};
RX PubMed=17303757; DOI=10.1126/science.1138438;
RA Newton I.L.G., Woyke T., Auchtung T.A., Dilly G.F., Dutton R.J.,
RA Fisher M.C., Fontanez K.M., Lau E., Stewart F.J., Richardson P.M.,
RA Barry K.W., Saunders E., Detter J.C., Wu D., Eisen J.A., Cavanaugh C.M.;
RT "The Calyptogena magnifica chemoautotrophic symbiont genome.";
RL Science 315:998-1000(2007).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; CP000488; ABL01827.1; -; Genomic_DNA.
DR RefSeq; WP_011737453.1; NC_008610.1.
DR AlphaFoldDB; A1AV70; -.
DR STRING; 413404.Rmag_0024; -.
DR KEGG; rma:Rmag_0024; -.
DR eggNOG; COG0739; Bacteria.
DR HOGENOM; CLU_026846_4_0_6; -.
DR OrthoDB; 9805070at2; -.
DR Proteomes; UP000002587; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF270; OUTER MEMBRANE ANTIGENIC LIPOPROTEIN B; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF19425; Csd3_N2; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
DR PROSITE; PS51782; LYSM; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..372
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002632036"
FT DOMAIN 27..75
FT /note="LysM"
FT /evidence="ECO:0000259|PROSITE:PS51782"
SQ SEQUENCE 372 AA; 42333 MW; 9139D9D1824E99FC CRC64;
MGKLYTNILL ILISFSIASA YANNNAYHFT IKRGDSLSQY FSKLGLSSRL LANLLFANKN
NKKLNQLTIG HKLTIRLSNN RQFKSLTYQL NRKTNLNVIL NNNYFSTILK KQSKQIPINL
SITVVRINHS FGVDAQKEGI GFSTINLIVK ALSRQLNFNT DLKKGDRFII VNNDNIKPVA
IIYQSIIKNK SIEAFAYKNK HGHTGYFDRF GHSLSSSFLK APLKYKRISS KFQLRRYHPI
LKTWRPHRAV DYAANYGTPV YSTANGIITT KDKKGALGKV VIIQHGFDYV TVYAHLSKYA
NNLYKDKKVK KGQIIGYVGS TGRSTGPHLH YELHYKGKRR NPLTYKLPAQ KGISRANLQD
FKIKVNKILS SL
//
