ID F3KRV8_9BURK Unreviewed; 382 AA.
AC F3KRV8;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Peptidase S49 {ECO:0000313|EMBL:EGI77442.1};
GN ORFNames=HGR_05936 {ECO:0000313|EMBL:EGI77442.1};
OS Hylemonella gracilis ATCC 19624.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hylemonella.
OX NCBI_TaxID=887062 {ECO:0000313|EMBL:EGI77442.1, ECO:0000313|Proteomes:UP000016368};
RN [1] {ECO:0000313|EMBL:EGI77442.1, ECO:0000313|Proteomes:UP000016368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19624 {ECO:0000313|EMBL:EGI77442.1,
RC ECO:0000313|Proteomes:UP000016368};
RX PubMed=21673657; DOI=10.1038/emboj.2011.186;
RA Chen S., Beeby M., Murphy G.E., Leadbetter J.R., Hendrixson D.R.,
RA Briegel A., Li Z., Shi J., Tocheva E.I., Muller A., Dobro M.J.,
RA Jensen G.J.;
RT "Structural diversity of bacterial flagellar motors.";
RL EMBO J. 30:2972-2981(2011).
CC -!- SIMILARITY: Belongs to the peptidase S49 family.
CC {ECO:0000256|ARBA:ARBA00008683}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGI77442.1}.
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DR EMBL; AEGR01000047; EGI77442.1; -; Genomic_DNA.
DR RefSeq; WP_006297196.1; NZ_AEGR01000047.1.
DR AlphaFoldDB; F3KRV8; -.
DR STRING; 887062.HGR_05936; -.
DR eggNOG; COG0616; Bacteria.
DR OrthoDB; 9764363at2; -.
DR Proteomes; UP000016368; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd07023; S49_Sppa_N_C; 1.
DR InterPro; IPR029045; ClpP/crotonase-like_dom_sf.
DR InterPro; IPR002142; Peptidase_S49.
DR InterPro; IPR047272; S49_SppA_C.
DR PANTHER; PTHR42987; PEPTIDASE S49; 1.
DR PANTHER; PTHR42987:SF4; PROTEASE SLR0021-RELATED; 1.
DR Pfam; PF01343; Peptidase_S49; 1.
DR SUPFAM; SSF52096; ClpP/crotonase; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022670};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000016368};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 102..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 198..342
FT /note="Peptidase S49"
FT /evidence="ECO:0000259|Pfam:PF01343"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 57..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 382 AA; 40367 MW; C2CC723ED1E53391 CRC64;
MNESSRDEPG FGDISASSSS SETSTAPAPL TAHPITADAE APGASDPKGG AGAAAKTSNS
KAASSTASAT ATAAEPGWER AVLEKLAFAS LNEQRAARRW KIANRMIFLF LFLLMLWLLF
RPSHPGTATP QKHTAVVSIR GEISSDSEAG ADLVLAAARE AFENTDAQAV VLLIDSPGGS
PVQAGIINDE ILRLKALHKK PVYAVVEESC ASAAYYIAVS ADRIFVDKAS IVGSIGVLMD
GFGFTGLMDK LGVERRLMTA GENKGFLDPF SPQTVSQREH AQAMLNQIHQ QFIAVVKAGR
GKRLQETPDT FSGLFWTGEQ AVQMGLADQL GSLGYVAREV VQAEALVDYT RTPNVAERLA
KRFGAAVGAG AVRALQLQPA LR
//
