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Database: UniProt
Entry: U1KNH2_9GAMM
LinkDB: U1KNH2_9GAMM
Original site: U1KNH2_9GAMM 
ID   U1KNH2_9GAMM            Unreviewed;       504 AA.
AC   U1KNH2;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   SubName: Full=Regulator {ECO:0000313|EMBL:ERG17553.1};
GN   ORFNames=PCIT_17665 {ECO:0000313|EMBL:ERG17553.1};
OS   Pseudoalteromonas citrea DSM 8771.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1117314 {ECO:0000313|EMBL:ERG17553.1, ECO:0000313|Proteomes:UP000016487};
RN   [1] {ECO:0000313|EMBL:ERG17553.1, ECO:0000313|Proteomes:UP000016487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 8771 {ECO:0000313|Proteomes:UP000016487};
RX   PubMed=22535931; DOI=10.1128/JB.00265-12;
RA   Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA   He H.L., Zhou B.C., Zhang Y.Z.;
RT   "Genome sequences of type strains of seven species of the marine bacterium
RT   Pseudoalteromonas.";
RL   J. Bacteriol. 194:2746-2747(2012).
CC   -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. ComM
CC       subfamily. {ECO:0000256|ARBA:ARBA00006354}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ERG17553.1}.
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DR   EMBL; AHBZ02000177; ERG17553.1; -; Genomic_DNA.
DR   AlphaFoldDB; U1KNH2; -.
DR   STRING; 1117314.PCIT_17665; -.
DR   eggNOG; COG0606; Bacteria.
DR   OrthoDB; 9813147at2; -.
DR   Proteomes; UP000016487; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0032508; P:DNA duplex unwinding; IEA:InterPro.
DR   Gene3D; 3.30.230.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR045006; CHLI-like.
DR   InterPro; IPR001208; MCM_dom.
DR   InterPro; IPR004482; Mg_chelat-rel.
DR   InterPro; IPR025158; Mg_chelat-rel_C.
DR   InterPro; IPR000523; Mg_chelatse_chII-like_cat_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020568; Ribosomal_Su5_D2-typ_SF.
DR   InterPro; IPR014721; Ribsml_uS5_D2-typ_fold_subgr.
DR   NCBIfam; TIGR00368; YifB family Mg chelatase-like AAA ATPase; 1.
DR   PANTHER; PTHR32039:SF7; COMPETENCE PROTEIN COMM; 1.
DR   PANTHER; PTHR32039; MAGNESIUM-CHELATASE SUBUNIT CHLI; 1.
DR   Pfam; PF13541; ChlI; 1.
DR   Pfam; PF01078; Mg_chelatase; 1.
DR   Pfam; PF13335; Mg_chelatase_C; 1.
DR   PRINTS; PR01657; MCMFAMILY.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF54211; Ribosomal protein S5 domain 2-like; 1.
DR   PROSITE; PS50051; MCM_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016487}.
FT   DOMAIN          291..349
FT                   /note="MCM"
FT                   /evidence="ECO:0000259|PROSITE:PS50051"
SQ   SEQUENCE   504 AA;  55169 MW;  AC1AF7877B9CE13C CRC64;
     MSLAKVYTRA QVGISAPEVT VEVHLSNGLP AFHIVGLPET SVKEARERVR SALTNSKFLF
     PEQRITVNLA PADLPKEGGR YDLAIAVGIL VASKQLQAFQ SHHYEFYGEL TLSGEVHSVH
     AILPAVLAAE KAQRCCYIPK GNDQVASLAQ HCNRKAVNSL QALWLDLQGQ DALPLNMKYP
     SVNTHSVGSP LDMSEVKGQS GAKRVLEIAA AGGHNTLFLG PPGTGKSMLA QRMPSIMPTL
     LNNEALETAA IYSLIGKAID IENWRNRPFR SPHHTCSAVA LVGGSSNPKP GEISLAHNGV
     LFLDELPEFE RKVLDSLREP METGLVTISR AARQVDFPAR FQLIAALNPS PTGSLSDKRA
     TPDQVLRYLS KISGPFLDRI DLQIELPRLT TQELQTETCA ESSETIRNRV NTAHRIAIER
     QGMCNALLGN KALSQFCKLG HAESQFLGAA TEKLNLSPRS YHRILKVART IADMAGRAQI
     DLIDIKEALS YRAFERLLSQ LTRY
//
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