eF-site ID 3ktg-ABCDEFG PDB Code 3ktg Chain A, B, C, D, E, F, G click to enlarge Title Structure of ClpP from Bacillus subtilis in monoclinic crystal form Classification HYDROLASE Compound ATP-dependent Clp protease proteolytic subunit Source Bacillus subtilis (CLPP_BACSU) Sequence A:  IPTVIAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFL AAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTI CIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQG QATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDR DNFKSAEEALEYGLIDKILTHLEHHHHH B:  IPTVIAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFL AAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTI CIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQG QATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDR DNFKSAEEALEYGLIDKILTHLEHHHHH C:  IPTVIAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFL AAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTI CIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQG QATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDR DNFKSAEEALEYGLIDKILTHLEHHHHH D:  IPTVIAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFL AAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTI CIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQG QATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDR DNFKSAEEALEYGLIDKILTHLEHHHHH E:  IPTVIAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFL AAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTI CIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQG QATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDR DNFKSAEEALEYGLIDKILTHLEHHHHH F:  IPTVIAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFL AAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTI CIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQG QATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDR DNFKSAEEALEYGLIDKILTHLEHHHHH G:  IPTVIAYDIYSRLLKDRIIMLGSAIDDNVANSIVSQLLFL AAEDPEKEISLYINSPGGSITAGMAIYDTMQFIKPKVSTI CIGMAASMGAFLLAAGEKGKRYALPNSEVMIHQPLGGAQG QATEIEIAAKRILLLRDKLNKVLAERTGQPLEVIERDTDR DNFKSAEEALEYGLIDKILTHLEHHHHH Description Functional site 1) chain A residue 97 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI1 2) chain B residue 97 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI1 3) chain C residue 97 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI1 4) chain D residue 97 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI1 5) chain E residue 97 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI1 6) chain F residue 97 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI1 7) chain G residue 97 type ACT_SITE sequence S description Nucleophile => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI1 8) chain A residue 122 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI2 9) chain B residue 122 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI2 10) chain C residue 122 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI2 11) chain D residue 122 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI2 12) chain E residue 122 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI2 13) chain F residue 122 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI2 14) chain G residue 122 type ACT_SITE sequence H description ACT_SITE => ECO:0000255|HAMAP-Rule:MF_00444, ECO:0000305|PubMed:22080375 source Swiss-Prot : SWS_FT_FI2 15) chain A residue 89-100 type prosite sequence TICIGMAASMGA description CLP_PROTEASE_SER Endopeptidase Clp serine active site. TicIGmAASMGA source prosite : PS00381 16) chain A residue 111-124 type prosite sequence RYALPNSEVMIHQP description CLP_PROTEASE_HIS Endopeptidase Clp histidine active site. RyalPnseVMIHQP source prosite : PS00382

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