ID A0A0H3GUR0_KLEPH Unreviewed; 423 AA.
AC A0A0H3GUR0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Peptidase M23 domain-containing protein {ECO:0000259|Pfam:PF01551};
GN OrderedLocusNames=KPHS_51170 {ECO:0000313|EMBL:AEW63815.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain HS11286).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=1125630 {ECO:0000313|EMBL:AEW63815.1, ECO:0000313|Proteomes:UP000007841};
RN [1] {ECO:0000313|EMBL:AEW63815.1, ECO:0000313|Proteomes:UP000007841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HS11286 {ECO:0000313|EMBL:AEW63815.1,
RC ECO:0000313|Proteomes:UP000007841};
RX PubMed=22408243; DOI=10.1128/JB.00043-12;
RA Liu P., Li P., Jiang X., Bi D., Xie Y., Tai C., Deng Z., Rajakumar K.,
RA Ou H.Y.;
RT "Complete genome sequence of Klebsiella pneumoniae subsp. pneumoniae
RT HS11286, a multidrug-resistant strain isolated from human sputum.";
RL J. Bacteriol. 194:1841-1842(2012).
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DR EMBL; CP003200; AEW63815.1; -; Genomic_DNA.
DR RefSeq; WP_002922458.1; NC_016845.1.
DR RefSeq; YP_005229417.1; NC_016845.1.
DR AlphaFoldDB; A0A0H3GUR0; -.
DR SMR; A0A0H3GUR0; -.
DR STRING; 1125630.KPHS_51170; -.
DR GeneID; 11850188; -.
DR KEGG; kpm:KPHS_51170; -.
DR PATRIC; fig|1125630.4.peg.5002; -.
DR HOGENOM; CLU_029425_4_0_6; -.
DR Proteomes; UP000007841; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007841};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..38
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 39..423
FT /note="Peptidase M23 domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002610445"
FT DOMAIN 324..417
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
FT REGION 212..233
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 44..127
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 217..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..281
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 423 AA; 46900 MW; ACC52C782645FF91 CRC64;
MRGKAMYSTT WIAAAVRSVL YASALSAGVL LCASSAHADD RDQLKSIQAD IAARQRAIKQ
QQQQRASLLA QLKAQEEAIA AAARKLRETQ DSLNQLNKQI DEMNAALAKL ERQRASQERN
LAAQLDAAFR QGPHTGIQMV LSGEEGQRNQ RMQVYFSYFN QARQETIAEL KKTREEMAVQ
KSMLEEKQSQ QQTLVYEQKA QQAKLEQARN ERKKTLSGLE SSIQQGQQQL SELRANESRL
RGRIAQAEAA AKARADREAR DAQAVRDRQQ EASRKGTTYK PTESERSLMS RTGGLGSPRG
QAFWPVRGPL LHRYGEQLQG ELRWKGMVIA ASEGTEVRAI ADGRVILADW LQGYGLVVVV
EHGKGDMSLY GYNQSALVSV GTQVRAGQPI ALVGSSGGQG RPSLYFEIRR QGQAVNPQPW
LGR
//
