ID D0LQ82_HALO1 Unreviewed; 621 AA.
AC D0LQ82;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Peptidyl-dipeptidase A {ECO:0000313|EMBL:ACY18891.1};
DE EC=3.4.15.1 {ECO:0000313|EMBL:ACY18891.1};
GN OrderedLocusNames=Hoch_6422 {ECO:0000313|EMBL:ACY18891.1};
OS Haliangium ochraceum (strain DSM 14365 / JCM 11303 / SMP-2).
OC Bacteria; Myxococcota; Polyangia; Haliangiales; Kofleriaceae; Haliangium.
OX NCBI_TaxID=502025 {ECO:0000313|EMBL:ACY18891.1, ECO:0000313|Proteomes:UP000001880};
RN [1] {ECO:0000313|EMBL:ACY18891.1, ECO:0000313|Proteomes:UP000001880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14365 / CIP 107738 / JCM 11303 / AJ 13395 / SMP-2
RC {ECO:0000313|Proteomes:UP000001880};
RX PubMed=21304682; DOI=10.4056/sigs.69.1277;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Ivanova N., Daum C., Lang E., Abt B., Kopitz M., Saunders E., Lapidus A.,
RA Lucas S., Glavina Del Rio T., Nolan M., Tice H., Copeland A., Cheng J.F.,
RA Chen F., Bruce D., Goodwin L., Pitluck S., Mavromatis K., Pati A.,
RA Mikhailova N., Chen A., Palaniappan K., Land M., Hauser L., Chang Y.J.,
RA Jeffries C.D., Detter J.C., Brettin T., Rohde M., Goker M., Bristow J.,
RA Markowitz V., Eisen J.A., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Haliangium ochraceum type strain (SMP-2).";
RL Stand. Genomic Sci. 2:96-106(2010).
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DR EMBL; CP001804; ACY18891.1; -; Genomic_DNA.
DR AlphaFoldDB; D0LQ82; -.
DR STRING; 502025.Hoch_6422; -.
DR KEGG; hoh:Hoch_6422; -.
DR eggNOG; COG1164; Bacteria.
DR HOGENOM; CLU_014364_3_0_7; -.
DR OrthoDB; 5241329at2; -.
DR Proteomes; UP000001880; 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:ACY18891.1};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000313|EMBL:ACY18891.1};
KW Protease {ECO:0000313|EMBL:ACY18891.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001880};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..621
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003010490"
FT REGION 25..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 621 AA; 69622 MW; 0A118020D967ACE2 CRC64;
MRSRDQLASV LAALSLLVGA GCGSGQSSSE TAASAAEDGD GEAAQSEQPS AADAQAFIDE
YERERYDLAR KQAQAAWVRA TYITDDTAAL AADVDVEMMA FSAAKAHEAQ RFADLPLDGE
LGRKLALIRL SETTPGPDAP EKREALAQAL NEMQRIYGTG KYCPSEGTCW NLTELSQRLA
KSRNPKELLE VWTGWRSVTA EMRGEFERFV ELANEGARDM GFDDLGALWR SKYDMQPDET
AAEVDRLWGQ VQPLYEQLHC YVRGKLSQQY GASVVPDEGA IPAHVLGNMW AQDWSYLSWL
VTPGGNRAQV SEITRALKAK RVDAVGMVRY AERFFVSLGM PELPQSFWDR SMLVRPRDRE
VECHASAWSL DWKEDLRIKM CIEINDEDFS TIHHELGHIY YDWAYKDQPI LFADSAHDGF
HEALGDTIAL SVTPSYLKEI GLVPRSSQND TAQLLDRALQ KVAFLPFGLL VDKWRWQVFS
GEVGPENYNE AWWKLREQYQ GVRPPSERSE SDFDPGAKYH VASNVPYLRY FLAHVLQFQL
HRSLCEAAGH EGPLHQCSIY GSKEAGAKLQ AMMELGASKP WPEALALITG DDQMDASAMI
EYFAPLMTWL EQQNQGRTCG Y
//
