ID   Q0APM8_MARMM            Unreviewed;       617 AA.
AC   Q0APM8;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   02-SEP-2026, entry version 93.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ABI65759.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ABI65759.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=Mmar10_1467 {ECO:0000313|EMBL:ABI65759.1};
OS   Maricaulis maris (strain MCS10) (Caulobacter maris).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Maricaulales; Maricaulaceae; Maricaulis.
OX   NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI65759.1, ECO:0000313|Proteomes:UP000001964};
RN   [1] {ECO:0000313|EMBL:ABI65759.1, ECO:0000313|Proteomes:UP000001964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10 {ECO:0000313|EMBL:ABI65759.1,
RC   ECO:0000313|Proteomes:UP000001964};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP000449; ABI65759.1; -; Genomic_DNA.
DR   RefSeq; WP_011643406.1; NC_008347.1.
DR   AlphaFoldDB; Q0APM8; -.
DR   STRING; 394221.Mmar10_1467; -.
DR   KEGG; mmr:Mmar10_1467; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_5; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000001964; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 1.
DR   FunFam; 1.10.1370.30:FF:000005; Angiotensin-converting enzyme; 1.
DR   Gene3D; 1.10.1370.30; -; 2.
DR   InterPro; IPR001548; Peptidase_M2.
DR   PANTHER; PTHR10514; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   PANTHER; PTHR10514:SF27; ANGIOTENSIN-CONVERTING ENZYME; 1.
DR   Pfam; PF01401; Peptidase_M2; 1.
DR   PRINTS; PR00791; PEPDIPTASEA.
DR   SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR   PROSITE; PS52011; PEPTIDASE_M2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ABI65759.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR601548-4};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ABI65759.1};
KW   Lipoprotein {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR601548-3};
KW   Palmitate {ECO:0000256|PROSITE-ProRule:PRU00303};
KW   Protease {ECO:0000313|EMBL:ABI65759.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001964};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|PROSITE-
KW   ProRule:PRU00303}; Zinc {ECO:0000256|PIRSR:PIRSR601548-3}.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..617
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT                   /id="PRO_5050005636"
FT   CHAIN           28..617
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004168361"
FT   ACT_SITE        387
FT                   /note="Proton acceptor 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-1"
FT   ACT_SITE        387
FT                   /note="Proton acceptor 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-11"
FT   ACT_SITE        516
FT                   /note="Proton donor 1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-1"
FT   ACT_SITE        516
FT                   /note="Proton donor 2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-11"
FT   BINDING         226
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-2"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-3"
FT   BINDING         386
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-8"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-3"
FT   BINDING         390
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-8"
FT   BINDING         414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-3"
FT   BINDING         414
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-8"
FT   BINDING         525
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-2"
FT   LIPID           20
FT                   /note="N-palmitoyl cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT   LIPID           20
FT                   /note="S-diacylglycerol cysteine"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00303"
FT   DISULFID        355..373
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-4"
FT   DISULFID        541..553
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601548-4"
SQ   SEQUENCE   617 AA;  68993 MW;  ACE52A4F3D9FD6E8 CRC64;
     MKRLMTGVAS GALLAVLAGC SAPNEPAADT QAAAPATASP VTVADAEQFL ADATTELREF
     SEFGARTAWV QNNFITYDTN WLLERMSTQG TEMAVRLATE TARFNELEMT TEMSRQMNVL
     RAGITLPAPS DSAAAARLSE LTTRMGSAYS TGLMEIDGEM VDHNELENIM RTSRDPEFLS
     HVWAGWRDSY NPEQMSTDYA EMVEIANAGA RDLGFSDLAE MWLSNYDMPA DEMEAEVERL
     WGQVEPLYEQ LHCAVRSELN GLYGDEVQAA EGPIRADLLG NMWAQSWAAL ADVASVSDAG
     PAYDLTQLLV DADYDQIRMV ETAETFFTSL GMEELPDTFW ERSLITQPRD RQVACHASAW
     NLDSVDDLRI KMCTRVNADD FVTVHHELGH NFYQRAYNQQ DFLFQGGAHD GFHEAIGDFI
     ALSVTPDYLV QIGLLDQADV PDASADLGLL MDTALDKIAF LPFAVMMDQW RWRVLRGEIQ
     PDSYNDAWWE LRESYQGIVP PVERGETAFD PGSKYHIANN VPYLRYFLSF IMQFQFHEAA
     CEMAGWEGPL HRCSIYGNEE VGARFSAMME MGASQPWPDA LEAFTGTREM DGSAIIAYFQ
     PLMTHLEEQN ATRDCGW
//