Y344_CHLMU
ID Y344_CHLMU Reviewed; 619 AA.
AC Q9PKW7;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Putative zinc metalloprotease TC_0344;
DE EC=3.4.24.-;
GN OrderedLocusNames=TC_0344;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC membrane protein {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}.
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DR EMBL; AE002160; AAF39205.1; -; Genomic_DNA.
DR PIR; H81712; H81712.
DR RefSeq; WP_010230221.1; NZ_CP027217.1.
DR AlphaFoldDB; Q9PKW7; -.
DR STRING; 243161.TC_0344; -.
DR EnsemblBacteria; AAF39205; AAF39205; TC_0344.
DR GeneID; 1246387; -.
DR KEGG; cmu:TC_0344; -.
DR eggNOG; COG0750; Bacteria.
DR HOGENOM; CLU_025778_0_0_0; -.
DR OMA; YSRIVGW; -.
DR OrthoDB; 1395197at2; -.
DR Proteomes; UP000000800; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR InterPro; IPR004387; Pept_M50_Zn.
DR InterPro; IPR008915; Peptidase_M50.
DR PANTHER; PTHR42837; PTHR42837; 2.
DR Pfam; PF02163; Peptidase_M50; 1.
DR PROSITE; PS00142; ZINC_PROTEASE; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Hydrolase; Membrane; Metal-binding;
KW Metalloprotease; Protease; Transmembrane; Transmembrane helix; Zinc.
FT CHAIN 1..619
FT /note="Putative zinc metalloprotease TC_0344"
FT /id="PRO_0000088435"
FT TRANSMEM 103..125
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 558..580
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 593..610
FT /note="Helical"
FT /evidence="ECO:0000255"
FT ACT_SITE 21
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10095"
SQ SEQUENCE 619 AA; 69100 MW; 14E8236004779AFF CRC64;
MTVIYFVLAA LALGFLILIH ELGHLLAAKA VGMTVESFSI GFGPALVRKK MGSIEYRIGA
IPFGGYVRIK GMDRNDKEIS EDREKTVYDI PGGFFSKSPW KRIFVLAAGP LANILVALFA
FGILYFSGGR TKPFSEHTSI VGWAHPSLEQ KGLRPGDRIF LCNGQVYSGN KMAFSSSLLD
RKLSLQGEHP AYFSEAESFS LDVPFNPSLE GVPCLGASYL LYRGSEPLPE KSPLIDAGLS
EGDRLVWMDG ALVFSGVQVS QILNEKKAFL RIERQGKIVF VRQSRVLAGD LQLTSYFKNE
LIDCQYEAGL KGKWASLYML PYIINSDGFV ESKINLLNTD QQSLDYHLEL GDRIVAVDGI
PVMSNADILR LVQDHRVSLI FQRMSSGQLS VLDQKAADKA FIDSYDMDDL LRVAGSVGEE
REVSHLGEYR LVTRVQPKPW VHIYSEELLD KQRALASKFR DEQEKRYYLE RIESEKQRIS
LGIPLKDLAV QYNPAPLVLM GESISDSLRT VKALGSGRLS PQWLSGPVGI VRILHTGWSM
GIPEALSWIG LISINLAVLN LLPIPVLDGG YILLCLWESV SRRRLNMRLI EKGLVPFMIL
LILFFVFLTL QDLSRVFIG