ID   A0A1T4XF22_9GAMM        Unreviewed;       572 AA.
AC   A0A1T4XF22;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   SubName: Full=D-alanyl-D-alanine carboxypeptidase, serine-type, PBP4 family {ECO:0000313|EMBL:SKA87808.1};
GN   ORFNames=SAMN02745130_02878 {ECO:0000313|EMBL:SKA87808.1};
OS   Thiothrix eikelboomii.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Thiotrichaceae; Thiothrix.
OX   NCBI_TaxID=92487 {ECO:0000313|EMBL:SKA87808.1, ECO:0000313|Proteomes:UP000190460};
RN   [1] {ECO:0000313|EMBL:SKA87808.1, ECO:0000313|Proteomes:UP000190460}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49788 {ECO:0000313|EMBL:SKA87808.1,
RC   ECO:0000313|Proteomes:UP000190460};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S13 family.
CC       {ECO:0000256|ARBA:ARBA00006096}.
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DR   EMBL; FUYB01000016; SKA87808.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4XF22; -.
DR   STRING; 92487.SAMN02745130_02878; -.
DR   OrthoDB; 9802627at2; -.
DR   Proteomes; UP000190460; Unassembled WGS sequence.
DR   GO; GO:0004185; F:serine-type carboxypeptidase activity; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR   Gene3D; 3.50.80.20; D-Ala-D-Ala carboxypeptidase C, peptidase S13; 1.
DR   Gene3D; 3.40.710.10; DD-peptidase/beta-lactamase superfamily; 1.
DR   InterPro; IPR012338; Beta-lactam/transpept-like.
DR   InterPro; IPR000667; Peptidase_S13.
DR   NCBIfam; TIGR00666; PBP4; 1.
DR   PANTHER; PTHR30023; D-ALANYL-D-ALANINE CARBOXYPEPTIDASE; 1.
DR   PANTHER; PTHR30023:SF0; PENICILLIN-SENSITIVE CARBOXYPEPTIDASE A; 1.
DR   Pfam; PF02113; Peptidase_S13; 2.
DR   PRINTS; PR00922; DADACBPTASE3.
DR   SUPFAM; SSF56601; beta-lactamase/transpeptidase-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   3: Inferred from homology;
KW   Carboxypeptidase {ECO:0000313|EMBL:SKA87808.1};
KW   Hydrolase {ECO:0000313|EMBL:SKA87808.1};
KW   Protease {ECO:0000313|EMBL:SKA87808.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190460};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..572
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012730238"
FT   REGION          84..133
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        87..102
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   572 AA;  62869 MW;  AF40592AF4E96813 CRC64;
     MLTLRLSVIA VCSALLSACG TAPAPRPIIP AAEDLTSAPP AQRYVAQQQQ QQVNAQRYNQ
     QLRWQEQQRA QQAQQAQEAQ RQEAALQRLA EQRREREQEA ENARQQQLAM QQRSRDLRAQ
     QRQRMERVQQ QFSTPPALNT YARQDSRPVA QFAAGRMYTG PGRFTRLPDQ VAGSLRASGV
     SEAGMGAYVR LAGGGQPALL TANADNPQTP ASTMKLVTTY AALGILGPDY RWPTEIYTNG
     NVTGGTLYGD VIIRGYGNPQ FAETDFRQML QALRARGINN IKGNLVADTG FFNVPYQDPG
     AFDGNANAAY NAQPEAILYQ ERGSCYEFKD LKGKIQKICP VMPSSAQARQ ALNVNLFGSF
     WKIWVGEMGG QMQGSFARAG TPASAQLVYT HRSRPLREII VEVNKDSNNV MARQILLSVG
     AKQLGAPGTP QKGAQAIGQW LESRGLAFPE LRLENGSGLS RIEQITPRHM GEMLVDAYNS
     PYRNDLMSSM AVLGVDGTLK NRMKNSSLAG RGRFKTGTLR DVRAIAGYLQ AADGQTYVVS
     ILHNDPRARA SVRGAHDDLI EWVFAGSRSF GY
//