ID C1DKS7_AZOVD Unreviewed; 342 AA.
AC C1DKS7;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Peptidase, S49 family {ECO:0000313|EMBL:ACO78929.1};
GN OrderedLocusNames=Avin_27550 {ECO:0000313|EMBL:ACO78929.1};
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710 {ECO:0000313|EMBL:ACO78929.1, ECO:0000313|Proteomes:UP000002424};
RN [1] {ECO:0000313|EMBL:ACO78929.1, 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).
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
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DR EMBL; CP001157; ACO78929.1; -; Genomic_DNA.
DR AlphaFoldDB; C1DKS7; -.
DR STRING; 322710.Avin_27550; -.
DR EnsemblBacteria; ACO78929; ACO78929; Avin_27550.
DR KEGG; avn:Avin_27550; -.
DR eggNOG; COG0616; Bacteria.
DR HOGENOM; CLU_070316_0_0_6; -.
DR OrthoDB; 5614232at2; -.
DR Proteomes; UP000002424; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR Gene3D; 6.20.330.10; -; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR013703; Peptidase_S49_N_proteobac.
DR InterPro; IPR047272; S49_SppA_C.
DR PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR PANTHER; PTHR42987:SF1; PROTEASE SOHB-RELATED; 1.
DR Pfam; PF01343; Peptidase_S49; 1.
DR Pfam; PF08496; Peptidase_S49_N; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 4..150
FT /note="Peptidase S49 N-terminal proteobacteria"
FT /evidence="ECO:0000259|Pfam:PF08496"
FT DOMAIN 154..297
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
SQ SEQUENCE 342 AA; 38524 MW; 8475E39FBCD24503 CRC64;
MAVEFFLDYA GFLAQTVTVV VAVLVILVAI AVLRSRSRHR GEGHLEVHRL NDFYKSLRES
LEQIVLDKDR LKTRRKAEAK AEKRERKEGK TKPRLFVLDF DGDIRASATD KLRHEVTAVL
SMAKPEDEVV LRLESGGGLV HSYGLAASQL VRIRQAGVPL TVCVDKVAAS GGYMMACIGD
RILSAPFAIL GSIGVVAQLP NVHRLLKRHD IDFEVLTAGE YKRTLTVFGE NTEKGREKFQ
EDLETTHELF KNFVARYRPQ LTIDEIATGE IWLGQSALEK QLVDELMTSD EYLAAKAGSA
ELFQLHYAER KSLQERFGLG AALAVDRVLL NWWERLSRSR YQ
//
