ID   A0A1X9YKS7_9SPHN        Unreviewed;       889 AA.
AC   A0A1X9YKS7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Peptidase M14 carboxypeptidase A domain-containing protein {ECO:0000259|Pfam:PF00246};
GN   ORFNames=KC8_18940 {ECO:0000313|EMBL:ARS29351.1};
OS   Sphingomonas sp. KC8.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingomonas.
OX   NCBI_TaxID=1030157 {ECO:0000313|EMBL:ARS29351.1, ECO:0000313|Proteomes:UP000194475};
RN   [1] {ECO:0000313|EMBL:ARS29351.1, ECO:0000313|Proteomes:UP000194475}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KC8 {ECO:0000313|EMBL:ARS29351.1};
RA   Chen Y.-L., Yu C.-P., Hu A., Lee T.-H., Yang F.-C., Ismail W., Wang P.-H.,
RA   Wang C.-H., Goh K.-S., Shih C.-J., Chiang Y.-R.;
RT   "Bacteria use an extradiol dioxygenase-mediated pathway to degrade natural
RT   estrogens in aquatic ecosystems.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M14 family.
CC       {ECO:0000256|ARBA:ARBA00005988}.
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DR   EMBL; CP016306; ARS29351.1; -; Genomic_DNA.
DR   RefSeq; WP_010127389.1; NZ_CP016306.1.
DR   AlphaFoldDB; A0A1X9YKS7; -.
DR   STRING; 1030157.GCA_000214335_00549; -.
DR   KEGG; spkc:KC8_18940; -.
DR   eggNOG; COG2866; Bacteria.
DR   OrthoDB; 9767214at2; -.
DR   Proteomes; UP000194475; Chromosome.
DR   GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   CDD; cd06240; M14-like; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR029062; Class_I_gatase-like.
DR   InterPro; IPR000834; Peptidase_M14.
DR   PANTHER; PTHR11705:SF91; CARBOXYPEPTIDASE A1 (PANCREATIC)-RELATED; 1.
DR   PANTHER; PTHR11705; PROTEASE FAMILY M14 CARBOXYPEPTIDASE A,B; 1.
DR   Pfam; PF00246; Peptidase_M14; 1.
DR   SUPFAM; SSF52317; Class I glutamine amidotransferase-like; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000194475};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..889
FT                   /note="Peptidase M14 carboxypeptidase A domain-containing
FT                   protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5011007197"
FT   DOMAIN          54..214
FT                   /note="Peptidase M14 carboxypeptidase A"
FT                   /evidence="ECO:0000259|Pfam:PF00246"
FT   REGION          678..703
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        678..692
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   889 AA;  97027 MW;  D13691150C0D8A71 CRC64;
     MKSYLVRSLA AAALASTMLQ AAPLLAETVP SPKSVLGQDV ASDYYLANYD ESLNYFRKLA
     ASSNRIKLVD AGKTTQGREM VYAIISSPEN LQKFEHYKEV SRRLGEARDL TDADARKLAH
     ESKVIVHIDG GMHASEVADH QLPIALAHHL LSAKNDAEVA AILDNVILVL WPTLNPDGQN
     MVVDWYRKNL GTPYETSRMP WLYQEYVGHD NNRDGYMLNM LESQVATRAQ QDYAPVIWYS
     HHQVAPFPAR IWMPPFADPV SSNISPNMRI WTNAIGTNMM TRFEKEQKPG AIAQAKFDNW
     YPGFLDYTHV FRNTISFFTE VSHDSATPKT YKVEEFPKAF RDLKAQIMYP SPWKGGLWRL
     KDSVDYMMTA SMSVLDTATK YREDLLFNRY QAARDTISQY AAEGPYAYVI SSGQADMPEA
     ALLAQKMIDH GLKVHQARTA INLGGVTYPA GSWVLLTDQP YARLAVELFE KQKYPDAILD
     GSGKPVDLPY DVTGWTLPLQ MGVRVDTIKT PLDARIKGQL GEIASAALPK SSIVGKGNVF
     ALSRKVNASF VAVNEILSKG GRIGLSTGAV TTDKGAETGA IIVEGISRAA LLPILEKQRI
     NATAMAAAPA VNGIAAAKVG LYRPWGANMY DEGWTRWLLE QSNYAPASIY NADMKAGSLS
     AKFDTIILPD INGPSAEKIA EEQRKKAAAG EKTSTRRPGP IGTLLDGLSS TDVPASYAGG
     IGDDGAAALK AFVADGGTLI ALNNASDAVI DLFDLPVTNI LKNAKSTEFF CSGALLEIGL
     NGASVATAGL PANPVVMFER GPAFEPKPGF NGQILASYAP DKNPLQSGVL LYPEKIQGKA
     AAMEVAYGKG KIYLYGFKPQ WRAQSHGTYK FLYNLLYKQK DDASTPAHH
//