ID F8L5I4_SIMNZ Unreviewed; 301 AA.
AC F8L5I4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE SubName: Full=Putative murein peptide carboxypeptidase {ECO:0000313|EMBL:CCB89476.1};
DE EC=3.4.16.- {ECO:0000313|EMBL:CCB89476.1};
GN Name=ykfA {ECO:0000313|EMBL:CCB89476.1};
GN OrderedLocusNames=SNE_A15990 {ECO:0000313|EMBL:CCB89476.1};
OS Simkania negevensis (strain ATCC VR-1471 / Z).
OC Bacteria; Chlamydiota; Chlamydiia; Parachlamydiales; Simkaniaceae;
OC Simkania.
OX NCBI_TaxID=331113 {ECO:0000313|EMBL:CCB89476.1, ECO:0000313|Proteomes:UP000000496};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Z;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S.A., Horn M.;
RT "Unity in variety -- the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 0:0-0(2011).
RN [2] {ECO:0000313|EMBL:CCB89476.1, ECO:0000313|Proteomes:UP000000496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-1471 / Z {ECO:0000313|Proteomes:UP000000496};
RX PubMed=21690563; DOI=10.1093/molbev/msr161;
RA Collingro A., Tischler P., Weinmaier T., Penz T., Heinz E., Brunham R.C.,
RA Read T.D., Bavoil P.M., Sachse K., Kahane S., Friedman M.G., Rattei T.,
RA Myers G.S., Horn M.;
RT "Unity in variety--the pan-genome of the Chlamydiae.";
RL Mol. Biol. Evol. 28:3253-3270(2011).
CC -!- SIMILARITY: Belongs to the peptidase S66 family.
CC {ECO:0000256|ARBA:ARBA00010233}.
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DR EMBL; FR872582; CCB89476.1; -; Genomic_DNA.
DR RefSeq; WP_013943942.1; NC_015713.1.
DR AlphaFoldDB; F8L5I4; -.
DR STRING; 331113.SNE_A15990; -.
DR MEROPS; S66.001; -.
DR KEGG; sng:SNE_A15990; -.
DR eggNOG; COG1619; Bacteria.
DR HOGENOM; CLU_034346_3_1_0; -.
DR OrthoDB; 9807329at2; -.
DR Proteomes; UP000000496; Chromosome gsn.131.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd07025; Peptidase_S66; 1.
DR Gene3D; 3.40.50.10740; Class I glutamine amidotransferase-like; 1.
DR Gene3D; 3.50.30.60; LD-carboxypeptidase A C-terminal domain-like; 1.
DR InterPro; IPR027461; Carboxypeptidase_A_C_sf.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR027478; LdcA_N.
DR InterPro; IPR040449; Peptidase_S66_N.
DR InterPro; IPR040921; Peptidase_S66C.
DR InterPro; IPR003507; S66_fam.
DR PANTHER; PTHR30237; MURAMOYLTETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR PANTHER; PTHR30237:SF2; MUREIN TETRAPEPTIDE CARBOXYPEPTIDASE; 1.
DR Pfam; PF02016; Peptidase_S66; 1.
DR Pfam; PF17676; Peptidase_S66C; 1.
DR PIRSF; PIRSF028757; LD-carboxypeptidase; 1.
DR SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR SUPFAM; SSF141986; LD-carboxypeptidase A C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|ARBA:ARBA00022645,
KW ECO:0000313|EMBL:CCB89476.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCB89476.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000000496};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825}.
FT DOMAIN 14..131
FT /note="LD-carboxypeptidase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02016"
FT DOMAIN 176..291
FT /note="LD-carboxypeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17676"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 207
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
FT ACT_SITE 276
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR028757-1"
SQ SEQUENCE 301 AA; 32977 MW; BDB430EB2FF228E7 CRC64;
MMIQPPPLQA GDTIAIVAPA SLSKKEGEVV ACVQSLEVKG FKVKLAGNLE SQWGSFCGTD
AERASGIMEA FQDEDVKAIW CLRGGYGSGR LLDQLDYDLI RQNPKIFIGM SDITALHVAL
NQKAELITYL GPNANFIFAT DEDRSFAEKH AWKVLLGVQE TLIFEGGETL VSGKATGELK
GGNLALLAAH VGTPWQIETK GKILLLEEVN EFSYRIDRML CQLKQAGLLD DIAGLILSSW
SGCDPQHPQD FNLNQVLKNY FENASYPVLL DFPSGHIENQ ATLPLGHVVE LDADLKTLKI
Y
//
