ID C1DJD5_AZOVD Unreviewed; 420 AA.
AC C1DJD5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE SubName: Full=Peptidase M23B family {ECO:0000313|EMBL:ACO76720.1};
GN OrderedLocusNames=Avin_04650 {ECO:0000313|EMBL:ACO76720.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO76720.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO76720.1, ECO:0000313|Proteomes:UP000002424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303 {ECO:0000313|Proteomes:UP000002424};
RX PubMed=19429624; DOI=10.1128/JB.00504-09;
RA Setubal J.C., dos Santos P., Goldman B.S., Ertesvag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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DR EMBL; CP001157; ACO76720.1; -; Genomic_DNA.
DR RefSeq; WP_012699148.1; NC_012560.1.
DR AlphaFoldDB; C1DJD5; -.
DR STRING; 322710.Avin_04650; -.
DR EnsemblBacteria; ACO76720; ACO76720; Avin_04650.
DR KEGG; avn:Avin_04650; -.
DR eggNOG; COG4942; Bacteria.
DR HOGENOM; CLU_029425_4_0_6; -.
DR OrthoDB; 9784703at2; -.
DR Proteomes; UP000002424; Chromosome.
DR CDD; cd12797; M23_peptidase; 1.
DR Gene3D; 6.10.250.3150; -; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF265; MUREIN HYDROLASE ACTIVATOR ENVC; 1.
DR PANTHER; PTHR21666; PEPTIDASE-RELATED; 1.
DR Pfam; PF01551; Peptidase_M23; 1.
DR SUPFAM; SSF51261; Duplicated hybrid motif; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..420
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002906347"
FT DOMAIN 319..412
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT REGION 247..291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 22..108
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 247..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 420 AA; 47872 MW; 83F8E20C590F487A CRC64;
MSRILPPLIL ALALSPAFAD ERSETLEQLE RARQDIATLK KLQEQLNRER SGVQQELGKT
EREMGDLENR VRELQNELDG REREIRRLDR EKQTLQETRD EQQRLIAVQT RATYQSGRQE
YLKLLLNQQR PELLSRTLAY YGYFDQARQR QLEALDATLR QLAAVEQDLA TQRTRLSERK
SELEERRERL AALRQERRRM LVRLNREYAS GARKLEAREE ERAELGRVLR RIEEALARQA
REAEEARQRA LAEQRRQQEQ ERQRQRASAP AGEAPLLSGR GTVPDGPFAR ARGSLPWPVD
GRLLVPYGSP RSEDARTRWD GVLISANAGT PVRAIHAGRV VFADWLRGSG LLVILDHGNG
YLSLYGHNES LLKSAGDMVK AGEPIATVGT SGGQDMPALY FAIRQQGHPS DPALWCRAQG
//
