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Database: UniProt
Entry: C6XNP7_HIRBI
LinkDB: C6XNP7_HIRBI
Original site: C6XNP7_HIRBI 
ID   C6XNP7_HIRBI            Unreviewed;       617 AA.
AC   C6XNP7;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ACT58300.1};
DE            EC=3.4.15.1 {ECO:0000313|EMBL:ACT58300.1};
GN   OrderedLocusNames=Hbal_0598 {ECO:0000313|EMBL:ACT58300.1};
OS   Hirschia baltica (strain ATCC 49814 / DSM 5838 / IFAM 1418).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomonadales;
OC   Hyphomonadaceae; Hirschia.
OX   NCBI_TaxID=582402 {ECO:0000313|EMBL:ACT58300.1, ECO:0000313|Proteomes:UP000002745};
RN   [1] {ECO:0000313|Proteomes:UP000002745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49814 / DSM 5838 / IFAM 1418
RC   {ECO:0000313|Proteomes:UP000002745};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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DR   EMBL; CP001678; ACT58300.1; -; Genomic_DNA.
DR   RefSeq; WP_015826450.1; NC_012982.1.
DR   AlphaFoldDB; C6XNP7; -.
DR   STRING; 582402.Hbal_0598; -.
DR   KEGG; hba:Hbal_0598; -.
DR   eggNOG; COG1164; Bacteria.
DR   HOGENOM; CLU_014364_3_0_5; -.
DR   OrthoDB; 5241329at2; -.
DR   Proteomes; UP000002745; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR   GO; GO:0008241; F:peptidyl-dipeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06461; M2_ACE; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Carboxypeptidase {ECO:0000313|EMBL:ACT58300.1};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW   Hydrolase {ECO:0000313|EMBL:ACT58300.1};
KW   Protease {ECO:0000313|EMBL:ACT58300.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002745};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..617
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002971531"
SQ   SEQUENCE   617 AA;  69501 MW;  BA0DB3931BB71B3D CRC64;
     MKKILLGSAA LLVAACASSQ MPWQKTEAVA EAPAASVAAP VLTVEDAETF ITAAEAELTE
     MGEYAARVYW LQATNINFDT NWLVSKVGAK YTQMAVRLAN GTKKYEDLDL PDELARKMSI
     LKAGITIPAP STDGVADELA NITTNLESTY STGTFEHNGE KLNLTQLSNI IAESRDPEEL
     ATVWAGWREI SKPMKSEYAR MVEIANEGAR ELGFSDTADM WLANYDMPSA DMEKEVERLW
     TQVEPLYDQL HCKVRADLNE KYGDDVQPAD GFIRADLLGN MWAQQWSNIY DIVGPETSGP
     SYDVTTKLEE KGYTPLKMVE TAENFFTSLG LEELPETFWE RSQITRPRDR EVVCHASAWD
     LDSKDDIRIK MCTQVNAEDF QTVHHELGHN YYQRAYKNQS TLHQGGAHDG FHEAIGDFLA
     LSITPSYLKD IGLIEESEIP DASADTGLLM NQALDKIAFL PFGLMVDKWR WEVFRGETTP
     EEYNDSWVKL RQQYQGITPP VERASDAFDP GAKYHIPGNT PYLRYFLSFV MQFQFHKAAC
     EMSGWEGPLH RCSIYNNKEV GEKFNAMMEM GASKPWPDAL EAFTGTREMD GSAIIEYFDP
     LMTYLKEENE GRACGWK
//
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