Y072_CHLTR
ID Y072_CHLTR Reviewed; 619 AA.
AC O84075;
DT 15-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Putative zinc metalloprotease CT_072;
DE EC=3.4.24.-;
GN OrderedLocusNames=CT_072;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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; AE001273; AAC67663.1; -; Genomic_DNA.
DR PIR; B71559; B71559.
DR RefSeq; NP_219575.1; NC_000117.1.
DR RefSeq; WP_009872359.1; NC_000117.1.
DR AlphaFoldDB; O84075; -.
DR STRING; 813.O172_00400; -.
DR EnsemblBacteria; AAC67663; AAC67663; CT_072.
DR GeneID; 884110; -.
DR KEGG; ctr:CT_072; -.
DR PATRIC; fig|272561.5.peg.81; -.
DR HOGENOM; CLU_025778_0_0_0; -.
DR InParanoid; O84075; -.
DR OMA; YSRIVGW; -.
DR Proteomes; UP000000431; 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; Reference proteome; Transmembrane;
KW Transmembrane helix; Zinc.
FT CHAIN 1..619
FT /note="Putative zinc metalloprotease CT_072"
FT /id="PRO_0000088437"
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; 69285 MW; BFFF42E478AC3F3F CRC64;
MTIIYFVLAA LALGFLILIH ELGHLLAAKA VGMSVESFSI GFGPALVRKK MGSVEYRIGA
IPFGGYVRIK GMDRNDKDNS GDKEKTVYDI PEGFFSKSPW KRIFVLAAGP LANLLVAIFV
FGILYFSGGR TKSFSEYTSI VGWVHPSLEQ QGLHAGDQIF FCNGQPYSGH KMAFSSSLLE
RKLSLQGQHP AYFSESEAFS LEAPFNPNME GVPCLGASYL LYRGSDPLPE KSPLVDAGLS
EGDRLVWMDG LLVFSGAQVS QMLNEKQSFL RVERQGKVVF VRQARVLAGD LTLTPYFKNE
LIDCQYEAGL KGKWASLYTL PYIINGDGFV ESKVKLLNDE RVSLDYNLEL GDKIVAVDGI
PVMSNADILR LVQDHRVSLI FQRMSPEQLT VLEQKAADQA FINSYDMDDL LRVAESVGEE
REVSRLGDYR LVTRVQPRPW AHIYSEALLD KQRALASKFR DEQERRYYLE RIEAEKQRIS
LGIPLKDLAV QYNPDPWVLM EESVSDSLKT VKALGMGRVS PQWLSGPVGI VRILHTGWSV
GIPEALAWIG LISVNLAVLN LLPIPVLDGG YILLCLWEIL SRRRLNMRLV EKALVPFMIL
LVLFFVFLTL QDLSRVFVG