ID A6TI99_KLEP7 Unreviewed; 245 AA.
AC A6TI99;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:ABR80322.1};
GN ORFNames=KPN_pKPN3p05943 {ECO:0000313|EMBL:ABR80322.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OG Plasmid pKPN3 {ECO:0000313|EMBL:ABR80322.1,
OG ECO:0000313|Proteomes:UP000000265}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR80322.1, ECO:0000313|Proteomes:UP000000265};
RN [1] {ECO:0000313|Proteomes:UP000000265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RC PLASMID=pKPN3 {ECO:0000313|Proteomes:UP000000265};
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004167}; Single-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004167}.
CC -!- SIMILARITY: Belongs to the peptidase M23B family.
CC {ECO:0000256|ARBA:ARBA00006646}.
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DR EMBL; CP000648; ABR80322.1; -; Genomic_DNA.
DR RefSeq; WP_004118669.1; NC_009649.1.
DR AlphaFoldDB; A6TI99; -.
DR EnsemblBacteria; ABR80322; ABR80322; KPN_pKPN3p05943.
DR GeneID; 64297914; -.
DR KEGG; kpn:KPN_pKPN3p05943; -.
DR HOGENOM; CLU_026846_1_1_6; -.
DR Proteomes; UP000000265; Plasmid pKPN3.
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; -; 1.
DR Gene3D; 2.70.70.10; Glucose Permease (Domain IIA); 1.
DR InterPro; IPR045834; Csd3_N2.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR016047; Peptidase_M23.
DR PANTHER; PTHR21666:SF291; MUREIN DD-ENDOPEPTIDASE MEPM; 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.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Plasmid {ECO:0000313|EMBL:ABR80322.1};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 7..110
FT /note="Csd3-like second N-terminal"
FT /evidence="ECO:0000259|Pfam:PF19425"
FT DOMAIN 122..215
FT /note="Peptidase M23"
FT /evidence="ECO:0000259|Pfam:PF01551"
SQ SEQUENCE 245 AA; 27082 MW; 56A173EA7AFB333F CRC64;
MYSTDVVKEN AYLSATRSGL ESNEIATLQR SLPSRFNLRH LKKNESLKLV LQKKAGKSRV
VAYKFTSGSF NYTAYRISDK KFYNLSDTSG KGSLDYPLPA TARLSSPFNP ARLNPVSGKV
SPHNGIDYSM PMNTKIVSVI DGKITRAEYN STMGYFVEVT GKAGVKTRYL HLNKILVTKG
ARVTRGDAIA LSGNSGRSSG PHLHYELVIN NNPVNSLAFR AAAPADNKLE QHAFAHARDY
ERYLD
//